Search

Your search keyword '"Claude Taillefumier"' showing total 100 results
Start Over Author "Claude Taillefumier"
100 results on '"Claude Taillefumier"'

1. First series of N-alkylamino peptoid homooligomers: solution phase synthesis and conformational investigation

Author

Maxime Pypec, Laurent Jouffret, Claude Taillefumier, and Olivier Roy

Subjects
cis/trans isomerism, peptoid, structure, trans-inducing side chain, Science, Organic chemistry, QD241-441
Abstract

The synthesis and conformational analysis of the first series of peptoid oligomers composed of consecutive N-(alkylamino)glycine units is investigated. We demonstrate that N-(methylamino)glycine homooligomers can be readily synthesized in solution using N-Boc-N-methylhydrazine as a peptoid submonomer and stepwise or segment coupling methodologies. Their structures were analyzed in solution by 1D and 2D NMR, in the solid state by X-ray crystallography (dimer 2), and implicit solvent QM geometry optimizations. N-(Methylamino)peptoids were found to preferentially adopt trans amide bonds with the side chain N–H bonds oriented approximately perpendicular to the amide plane. This orientation is conducive to local backbone stabilization through intra-residue hydrogen bonds but also to intermolecular associations. The high capacity of N-(methylamino)peptoids to establish intermolecular hydrogen bonds was notably deduced from pronounced concentration-dependent N–H chemical shift variation in 1H NMR and the antiparallel arrangement of mirror image molecules held together via two hydrogen bonds in the crystal lattice of dimer 2.

Published
2022
Full Text
View/download PDF

2. Unveiling the conformational landscape of achiral all- cis tert -butyl β-peptoids

Author

Gaetano Angelici, Nicholus Bhattacharjee, Maxime Pypec, Laurent Jouffret, Claude Didierjean, Franck Jolibois, Lionel Perrin, Olivier Roy, Claude Taillefumier, Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie de Clermont-Ferrand (ICCF), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA)-Institut national polytechnique Clermont Auvergne (INP Clermont Auvergne), and Université Clermont Auvergne (UCA)-Université Clermont Auvergne (UCA)

Subjects
Organic Chemistry, [CHIM]Chemical Sciences, Physical and Theoretical Chemistry, Biochemistry
Abstract

The synthesis of β-peptoids with tert-butyl side chains up to 15 residues in length was achieved. Their backbone is characterized by cis-amide bonds, leading to helix and ribbon-like structures.

Published
2022

3. First series of

Author

Maxime, Pypec, Laurent, Jouffret, Claude, Taillefumier, and Olivier, Roy

Abstract

The synthesis and conformational analysis of the first series of peptoid oligomers composed of consecutive

Published
2022

4. Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide cis-Inducing NtBu Monomers

Author

Claude Taillefumier, Olivier Roy, Maha Rzeigui, Laurent Jouffret, Mounir Traïkia, Jameleddine Khiari, Alexandre Kriznik, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), SIGMA Clermont (SIGMA Clermont), Université de Carthage - University of Carthage, Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Ingénierie, Biologie et Santé en Lorraine (IBSLor), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), GONNET, JULIE, and Université de Lorraine (UL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
010405 organic chemistry, Peptidomimetic, Stereochemistry, Organic Chemistry, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Sequence (biology), Peptoid, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, 010402 general chemistry, 01 natural sciences, 0104 chemical sciences, Folding (chemistry), chemistry.chemical_compound, Monomer, chemistry, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Amide, Side chain, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Polyproline helix
Abstract

International audience; The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However, cis-trans isomerization of the backbone tertiary amides may impair the peptoid's adoption of stable secondary structures, notably the all-cis polyproline I-like helical conformation. Here, we show that cis-inducing NtBu achiral monomers strategically positioned within chiral sequences may reinforce the degree of peptoid helicity, although with a reduced content of chiral side chains. The design principles presented here will undoubtedly help achieve more conformationally stable helical peptoids with desired functions.

Published
2019

5. Solution‐Phase Synthesis of Backbone‐Constrained Cationic Peptoid Hexamers with Antibacterial and Anti‐biofilm Activities

Author

Sophie Faure, Nicolas Charbonnel, Christiane Forestier, Radhe Shyam, Claude Taillefumier, Olivier Roy, Laboratoire Microorganismes : Génome et Environnement (LMGE), Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA), Institut de Chimie de Clermont-Ferrand (ICCF), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA)-Institut national polytechnique Clermont Auvergne (INP Clermont Auvergne), Université Clermont Auvergne (UCA)-Université Clermont Auvergne (UCA), French Government IDEX-ISITE initiative 16-IDEX-0001 (CAP20–25), and ANR-13-BS07-0008,ArchiPep,Nouveaux édifices peptoïdes: de leur structure à leur application biologique(2013)

Subjects
010405 organic chemistry, Peptidomimetic, Organic Chemistry, Cationic polymerization, Peptoid, 010402 general chemistry, 01 natural sciences, Combinatorial chemistry, 0104 chemical sciences, chemistry.chemical_compound, chemistry, Amphiphile, [CHIM]Chemical Sciences, Physical and Theoretical Chemistry, Solution phase synthesis, Anti biofilm, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2021

6. Design, Synthesis, and Immunological Evaluation of a Multicomponent Construct Based on a Glycotripeptoid Core Comprising B and T Cell Epitopes and a Toll-like Receptor 7 Agonist That Elicits Potent Immune Responses

Author

Aurélie Job, Richard Lo-Man, Thomas Szekely, Olivier Roy, Claude Leclerc, Claude Taillefumier, Edith Dériaud, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Régulation Immunitaire et Vaccinologie, Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), This work was supported by funding from the French Ministry of Higher Education and Research (MESR to T.S.) for the chemical syntheses and by the Ligue Nationale Contre le Cancer (Equipe Labellisée 2017) to C.L. for the immunological analyses., and Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)

Subjects
Agonist, medicine.drug_class, Epitopes, T-Lymphocyte, Chemistry Techniques, Synthetic, 010402 general chemistry, 01 natural sciences, Epitope, Mice, Immune system, Adjuvanticity, Drug Discovery, medicine, Animals, [CHIM]Chemical Sciences, Amino Acid Sequence, Receptor, Toll-like receptor, biology, 010405 organic chemistry, Chemistry, TLR7, 3. Good health, 0104 chemical sciences, Mice, Inbred C57BL, Toll-Like Receptor 7, Drug Design, Immunology, biology.protein, Epitopes, B-Lymphocyte, Molecular Medicine, Peptidomimetics, Antibody
Abstract

International audience; We present here for the first time the synthesis and immunological evaluation of a fully synthetic three-component anticancer vaccine candidate that consists of a β-glycotripeptoid core mimicking a cluster of Tn at the surface of tumor cells (B epitope), conjugated to the OVA 323–339 peptide (T-cell epitope) and a Toll-like receptor 7 (TLR7) agonist for potent adjuvanticity. The immunological evaluation of this construct and of precursor components demonstrated the synergistic activity of the components within the conjugate to stimulate innate and adaptive immune cells (DCs, T-helper, and B-cells). Surprisingly, immunization of mice with the tricomponent GalNAc-based construct elicited a low level of anti-Tn IgG but elicited a very high level of antibodies that recognize the TLR7 agonist. This finding could represent a potential vaccine therapeutic approach for the treatment of some autoimmune diseases such as lupus.

Published
2018

7. Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide

Author

Maha, Rzeigui, Mounir, Traikia, Laurent, Jouffret, Alexandre, Kriznik, Jameleddine, Khiari, Olivier, Roy, and Claude, Taillefumier

Abstract

The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However

Published
2019

8. 1,2,3-Triazolium-Based Peptoid Oligomers

Author

Mohamed Zouikri, Hafida Aliouat, Claude Taillefumier, Sophie Faure, Olivier Roy, Cécile Caumes, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Université Saâd Dahlab Blida 1 (UB1), and Université de Saâd Dahlab [Blida] (USDB )

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Chemistry, Stereochemistry, Organic Chemistry, Peptoid, Sequence (biology), 010402 general chemistry, 01 natural sciences, 0104 chemical sciences, Solvent, chemistry.chemical_compound, Amide, Propargyl, Side chain, [CHIM]Chemical Sciences, Alkyl
Abstract

International audience; The cis-directing effect of the 1,2,3-triazolium-type side chain was studied on dimeric peptoid models with various patterns: αα, αβ, βα and ββ. Low influences of the sequence and of the solvent were observed, the cis conformation of the amide carrying the triazolium ranging from 83 to 94% in proportion. The synthesis of peptoid homooligomers with four or eight pendant 1,2,3-triazolium side chains is described. α-, β- and α,β-peptoids carrying propargyl groups were subjected to CuAAC reaction using alkyl azides, and the resulting triazoles were quaternized providing well-defined multitriazolium platforms. The influence of the counteranion (PF6–, BF4– or I–) on the conformation was also studied.

Published
2017

9. NCα‐gem‐dimethylated peptoid side chains: A novel approach for structural control and peptide sequence mimetics

Author

Sophie Faure, Radhe Shyam, Gaetano Angelici, Lionel Nauton, Olivier Roy, Claude Taillefumier, Institut de Chimie de Clermont-Ferrand (ICCF), and SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS)

Subjects
Molecular model, Stereochemistry, Biophysics, Context (language use), Trimer, Peptide, Molecular Dynamics Simulation, 010402 general chemistry, 01 natural sciences, Biochemistry, Methylation, Protein Structure, Secondary, Biomaterials, chemistry.chemical_compound, Peptoids, Isomerism, Side chain, [CHIM]Chemical Sciences, Amino Acid Sequence, Amines, Peptide sequence, Nuclear Magnetic Resonance, Biomolecular, Polyproline helix, chemistry.chemical_classification, 010405 organic chemistry, Organic Chemistry, Peptoid, General Medicine, 0104 chemical sciences, chemistry, Peptides
Abstract

International audience; The design of linear peptoid oligomers adopting well‐defined secondary structures while mimicking defined peptide primary sequences is a major challenge in the context of drug discovery. To this end, chemists have developed cis‐inducing peptoid side chains to build robust polyproline type I helices. However, the number of efficient examples remains scarce and chemical diversity accessible through the use of these side chains is limited. Herein, we introduce an array of NCα‐gem‐dimethylated peptoid residues mimicking proteinogenic amino acids. Submonomer synthesis and block‐coupling approaches were explored to access heterooligomers incorporating these novel types of side chains. NMR studies of monomer and trimer models showed that the NCα‐gem‐dimethylated groups exert complete cis control on the backbone amide conformation. Lastly, a preliminary molecular modeling study gave an insight into the preferred orientation of the substituents of the NCα‐gem‐dimethyl side chains relative to the peptoid backbone.

Published
2019

10. Peptoid-phthalocyanine architectures with different grafting positions: Synthetic strategy and photoproperties

Author

Claude Taillefumier, Jameleddine Khiari, Fabienne Dumoulin, Omer Goler, Tuğba Küçük, Devrim Atilla, Olivier Roy, Zeynel Şahin, Maha Rzeigui, Institut de Chimie de Clermont-Ferrand (ICCF), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA)-Institut national polytechnique Clermont Auvergne (INP Clermont Auvergne), and Université Clermont Auvergne (UCA)-Université Clermont Auvergne (UCA)

Subjects
Conjugate, Helix, Zn-phthalocyanine, Process Chemistry and Technology, General Chemical Engineering, Phthalocyanine, Peptoid, 02 engineering and technology, 010402 general chemistry, 021001 nanoscience & nanotechnology, Grafting, 01 natural sciences, Cycloaddition, 0104 chemical sciences, Spatial geometry, Crystallography, chemistry.chemical_compound, chemistry, [CHIM]Chemical Sciences, 0210 nano-technology
Abstract

International audience; A monoazido Zn phthalocyanine has been grafted onto three different alkynyl-functionalized peptoid helices using copper-catalyzed azide–alkyne cycloaddition, demonstrating the feasibility of such conjugates. Their photoproperties have been examined relatively to the spatial geometry induced by the peptoid helix.

Published
2021

11. 1,2,3-Triazolium-Based Cationic Amphipathic Peptoid Oligomers Mimicking Antimicrobial Helical Peptides

Author

Radhe Shyam, Claude Taillefumier, Christelle Blavignac, Nicolas Charbonnel, Christiane Forestier, Aurélie Job, Sophie Faure, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA), Centre Imagerie Cellulaire Santé (CICS), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), and ANR-16-IDEX-0001,CAP 20-25,CAP 20-25(2016)

Subjects
Staphylococcus aureus, Peptidomimetic, Stereochemistry, Polymers, Antimicrobial peptides, Peptide, Microbial Sensitivity Tests, Random hexamer, 010402 general chemistry, 01 natural sciences, Biochemistry, Oligomer, chemistry.chemical_compound, Peptoids, Solid-phase synthesis, Drug Discovery, Amphiphile, Enterococcus faecalis, Escherichia coli, [CHIM]Chemical Sciences, General Pharmacology, Toxicology and Pharmaceutics, Pharmacology, chemistry.chemical_classification, 010405 organic chemistry, Circular Dichroism, Organic Chemistry, Molecular Mimicry, Peptoid, Triazoles, 0104 chemical sciences, chemistry, Microscopy, Electron, Scanning, Molecular Medicine, Antimicrobial Cationic Peptides
Abstract

International audience; Amphipathic cationic peptoids (N‐substituted glycine oligomers) represent a promising class of antimicrobial peptide mimics. The aim of this study is to explore the potential of the triazolium group as a cationic moiety and helix inducer to develop potent antimicrobial helical peptoids. Herein we report the first solid‐phase synthesis of peptoid oligomers incorporating 1,2,3‐triazolium‐type side chains and their evaluation against Escherichia coli, Enterococcus faecalis, and Staphylococcus aureus. Several triazolium‐based oligomers, even of short length, selectively kill bacteria over mammalian cells. SEM visualization of S. aureus cells treated with a dodecamer and a hexamer reveals severe cell membrane damage and suggests that the longer oligomer acts by pore formation.

Published
2018

12. Exploring the Conformation of Mixed Cis – Trans α,β-Oligopeptoids: A Joint Experimental and Computational Study

Author

Claude Taillefumier, Nicholus Bhattacharjee, Geoffrey Dumonteil, Olivier Roy, Franck Jolibois, Lionel Perrin, Laurent Jouffret, Gaetano Angelici, Sophie Faure, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Laboratoire de physique et chimie des nano-objets (LPCNO), Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC), Interface Theory Experiment : Mechanism & Modeling (ITEMM), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Department of Chemistry and Industrial Chemistry, University of Pisa, Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Pisa - Università di Pisa, Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie de Toulouse (ICT-FR 2599), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie Organique et Analytique (ICOA), Université d'Orléans (UO)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Toulouse (Université de Toulouse), Institut de Chimie de Clermont-Ferrand - Clermont Auvergne (ICCF), Sigma CLERMONT (Sigma CLERMONT)-Université Clermont Auvergne (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UPS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Laboratoire de structure et de dynamique des systèmes moléculaires et solides (LSDSMS), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2), Synthèse et étude de systèmes à intêret biologique (SEESIB), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Spectrometry, Mass, Electrospray Ionization, Molecular model, Stereochemistry, Proton Magnetic Resonance Spectroscopy, Molecular Conformation, Sequence (biology), Molecular Dynamics Simulation, Crystallography, X-Ray, 010402 general chemistry, 01 natural sciences, Peptoids, chemistry.chemical_compound, Biopolymers, Side chain, [CHIM]Chemical Sciences, Computer Simulation, Carbon-13 Magnetic Resonance Spectroscopy, ComputingMilieux_MISCELLANEOUS, 010405 organic chemistry, Organic Chemistry, Acetylation, Peptoid, 0104 chemical sciences, Monomer, chemistry, Intramolecular force, Quantum Theory, Two-dimensional nuclear magnetic resonance spectroscopy, Cis–trans isomerism
Abstract

International audience; The synthesis and conformational preferences of a set of new synthetic foldamers that combine both the α,β-peptoid backbone and side chains that alternately promote cis- and trans-amide bond geometries have been achieved and addressed jointly by experiment and molecular modeling. Four sequence patterns were thus designed and referred to as cis-β-trans-α, cis-α-trans-β, trans-β-cis-α, and trans-α-cis-β. α- and βNtBu monomers were used to enforce cis-amide bond geometries and α- and βNPh monomers to promote trans-amides. NOESY and molecular modeling reveal that the trans-α-cis-β and cis-β-trans-α tetramers show a similar pattern of intramolecular weak interactions. The same holds for the cis-α-trans-β and trans-β-cis-α tetramers, but the interactions are different in nature than those identified in the trans-α-cis-β-based oligomers. Interestingly, the trans-α-cis-β peptoid architecture allows establishment of a larger amount of structure-stabilizing intramolecular interactions.

Published
2018

13. Homogeneous and Robust Polyproline Type I Helices from Peptoids with Nonaromatic α-Chiral Side Chains

Author

Geoffrey Dumonteil, Alexandre Kriznik, Olivier Roy, Laurent Jouffret, Claude Taillefumier, Sophie Faure, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), and Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Pentamer, Stereochemistry, Peptoid, Peptide, General Chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Oligomer, Catalysis, 0104 chemical sciences, chemistry.chemical_compound, Colloid and Surface Chemistry, Monomer, chemistry, Helix, Side chain, [CHIM]Chemical Sciences, Polyproline helix
Abstract

International audience; Peptoids that are oligomers of N-substituted glycines represent a class of peptide mimics with great potential in areas ranging from medicinal chemistry to biomaterial science. Controlling the equilibria between the cis and trans conformations of their backbone amides is the major hurdle to overcome for the construction of discrete folded structures, particularly for the development of all-cis polyproline type I (PPI) helices, as tools for modulating biological functions. The prominent role of backbone to side chain electronic interactions (n → π*) and side chains bulkiness in promoting cis-amides was essentially investigated with peptoid aromatic side chains, among which the chiral 1-naphthylethyl (1npe) group yielded the best results. We have explored for the first time the possibility to achieve similar performances with a sterically hindered α-chiral aliphatic side chain. Herein, we report on the synthesis and detailed conformational analysis of a series of (S)-N-(1-tert-butylethyl)glycine (Ns1tbe) peptoid homo-oligomers. The X-ray crystal structure of an Ns1tbe pentamer revealed an all-cis PPI helix, and the CD curves of the Ns1tbe oligomers also resemble those of PPI peptide helices. Interestingly, the CD data reported here are the first for any conformationally homogeneous helical peptoids containing only α-chiral aliphatic side chains. Finally we also synthesized and analyzed two mixed oligomers composed of NtBu and Ns1tbe monomers. Strikingly, the solid state structure of the mixed oligomer Ac-(tBu)2-(s1tbe)4-(tBu)2-COOtBu, the longest to be solved for any linear peptoid, revealed a PPI helix of great regularity despite the presence of only 50% of chiral side chain in the sequence.

Published
2017

14. Antioxidant activities of peptoid-grafted chitosan films

Author

Olivier Roy, S. Badel, Pierre-Henri Elchinger, Claude Taillefumier, Thierry Bernardi, Philippe Michaud, Sophie Faure, Cédric Delattre, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Institut Pascal (IP), SIGMA Clermont (SIGMA Clermont)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), BioFilm Control, Biopôle Clermont Limagne, Saint-Beauzire, and SIGMA Clermont (SIGMA Clermont)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])

Subjects
Antioxidant, DPPH, medicine.medical_treatment, Bioengineering, macromolecular substances, 010402 general chemistry, 01 natural sciences, Applied Microbiology and Biotechnology, Biochemistry, Antioxidants, Chitosan, chemistry.chemical_compound, Peptoids, Picrates, medicine, Organic chemistry, Humans, [CHIM]Chemical Sciences, Chelation, Molecular Biology, 010405 organic chemistry, Chemistry, Hydroxyl Radical, Biphenyl Compounds, Food Packaging, technology, industry, and agriculture, Peptoid, General Medicine, equipment and supplies, 0104 chemical sciences, carbohydrates (lipids), Oxidative Stress, Covalent bond, Surface modification, Hydroxyl radical, Antioxidant Chitosan film Grafting Biosourced material Peptoid Polysaccharide, Oxidation-Reduction, Biotechnology
Abstract

International audience; The aim of this study was to investigate the possibility of immobilizing peptoid on chitosan film in order to generate new active material. Chitosan films have been grafted for the first time with short-length peptoid oligomers displaying antioxidant activities. The antioxidant activity of the selected peptoids was initially investigated with the DPPH assay and hydroxyl radical procedure. The metal chelating capacity of peptoids was also evaluated prior to their covalent attachment to chitosan. The benefit of chitosan functionalization with respect to its intrinsic antioxidant properties was finally evaluated in the present study. Interestingly, an increase of up to 90 % of the antioxidant activity of chitosan was observed.

Published
2017

15. From Glycopeptides to Glycopeptoids

Author

Claude Taillefumier, Sophie Faure, Thomas Szekely, and Olivier Roy

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Peptidomimetic, Glycoconjugate, Stereochemistry, Organic Chemistry, 010402 general chemistry, 01 natural sciences, Oligomer, Combinatorial chemistry, Glycopeptide, 0104 chemical sciences, 3. Good health, chemistry.chemical_compound, chemistry, Amide, Physical and Theoretical Chemistry
Abstract

This review covers the published literature describing the synthesis of glycopeptoids, a family of glycopeptide mimics. Members of this family are composed of an N-substituted glycine or β-alanine oligomer backbone linked to one or several carbohydrate moieties at the amide nitrogen atoms. The interest in this class of biomimetics lies in their enhanced proteolytic stability and greater conformational flexibility relative to glycopeptides. This Microreview not only describes the different methods for synthesising glycopeptoids but also discusses their application both as glycopeptidomimetics and glycocluster constructs.

Published
2014

16. Correction: Weak backbone CH⋯O=C and side chain tBu⋯tBu London interactions help promote helix folding of achiral NtBu peptoids

Author

Olivier Roy, Sophie Faure, Claude Taillefumier, Franck Jolibois, Lionel Perrin, Nicholus Bhattacharjee, Gaetano Angelici, Claude Didierjean, Laurent Jouffret, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de physique et chimie des nano-objets (LPCNO), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Interface Theory Experiment : Mechanism & Modeling (ITEMM), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
chemistry.chemical_classification, Double bond, 010405 organic chemistry, Chemistry, Stereochemistry, Metals and Alloys, General Chemistry, 010402 general chemistry, 01 natural sciences, Catalysis, 3. Good health, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Folding (chemistry), Helix, Materials Chemistry, Ceramics and Composites, Side chain, [CHIM.CRIS]Chemical Sciences/Cristallography
Abstract

Correction for ‘Weak backbone CH⋯OC and side chain tBu⋯tBu London interactions help promote helix folding of achiral NtBu peptoids’ by G. Angelici et al., Chem. Commun., 2016, 52, 4573–4576.

Published
2016

17. Weak backbone CH···O=C and side chain tBu···tBu London interactions help promote helix folding of achiral NtBu peptoids

Author

Claude Didierjean, Gaetano Angelici, Sophie Faure, Laurent Jouffret, Olivier Roy, Nicholus Bhattacharjee, Claude Taillefumier, Franck Jolibois, Lionel Perrin, Institut de Chimie de Clermont-Ferrand (ICCF), Institut de Chimie du CNRS (INC)-SIGMA Clermont (SIGMA Clermont)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), Laboratoire de physique et chimie des nano-objets (LPCNO), Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées, Interface Theory Experiment : Mechanism & Modeling (ITEMM), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut de Chimie de Toulouse (ICT), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes (IRSAMC), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Angelici, G., Bhattacharjee, N., Roy, O., Faure, S., Didierjean, C., Jouffret, L., Jolibois, F., Perrin, L., Taillefumier, C., Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Sigma CLERMONT (Sigma CLERMONT)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UPS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
Models, Molecular, Materials Chemistry2506 Metals and Alloys, Protein Folding, Magnetic Resonance Spectroscopy, Molecular model, Stereochemistry, Proton Magnetic Resonance Spectroscopy, Surfaces, Coatings and Film, Ceramics and Composite, 010402 general chemistry, Crystallography, X-Ray, Peptides, Stereoisomerism, Chemistry (all), Catalysis, Ceramics and Composites, Electronic, Optical and Magnetic Materials, Surfaces, Coatings and Films, 2506, 01 natural sciences, Catalysi, Coatings and Films, chemistry.chemical_compound, Models, Amide, Materials Chemistry, Side chain, Electronic, [CHIM]Chemical Sciences, Optical and Magnetic Materials, Crystallography, 010405 organic chemistry, Hydrogen bond, Chemistry, Electronic, Optical and Magnetic Material, Metals and Alloys, Molecular, Peptoid, General Chemistry, Nuclear magnetic resonance spectroscopy, 0104 chemical sciences, Folding (chemistry), Surfaces, Helix, Peptide, X-Ray
Abstract

International audience; The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. Analyses reveal that the folding of these oligomers is driven by weak CH⋯O[double bond, length as m-dash]C hydrogen bonding along the peptoid backbone and London interaction between tBu⋯tBu side-chains.

Published
2016

18. Synthesis of new C-glycosyl aza-β3-amino acids building blocks

Author

Yves Chapleur, Anne-Sophie Felten, Manuel Andreini, Nadia Pellegrini-Moïse, Hoang-Trang Tran Thien, Claude Taillefumier, Structure et Réactivité des Systèmes Moléculaires Complexes (SRSMC), Institut de Chimie du CNRS (INC)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
chemistry.chemical_classification, animal structures, Stereochemistry, Organic Chemistry, macromolecular substances, beta-amino-acid Aza-beta-peptide C-glycosyl compounds Chiral building block, Biochemistry, Reductive amination, Amino acid, carbohydrates (lipids), chemistry.chemical_compound, chemistry, Drug Discovery, [CHIM]Chemical Sciences, Organic chemistry, lipids (amino acids, peptides, and proteins), Glycosyl
Abstract

International audience; New C-glycosylated Nb-protected aza-beta3-amino acid building blocks have been prepared from C-glycosyl aldehydes of gluco and galacto configuration by reductive amination and subsequent N-alkylation. These moieties were elaborated to b-dipeptides by elongation at the C- or the N-terminus establishing their ability to be incorporated in original glycosylated foldamers.

Published
2012

19. Synthesis and binding affinities for sst receptors of cyclic peptoid SRIF-mimetics

Author

Denis Servent, Cécile Caumes, Olivier Roy, Morgane Reynaud, Sophie Faure, Thomas Hjelmgaard, and Claude Taillefumier

Subjects
Pharmacology, Somatostatin receptor, Stereochemistry, Organic Chemistry, Pharmaceutical Science, Binding potential, Peptoid, Biochemistry, Combinatorial chemistry, Small molecule, In vitro, chemistry.chemical_compound, Somatostatin, chemistry, Drug Discovery, Molecular Medicine, Pharmacophore, Receptor
Abstract

Mimicking the tetradecapeptide somatostatin through the design of novel non-peptide small molecules is needed for developing analogues with selective or universal affinity for human somatostatin receptors (hsst1–5) and improved pharmacological properties. We report the synthesis and evaluation of the binding potential of the first all-peptoid SRIF (somatotropin release-inhibiting factor) analogues. Cyclic β and mixed α/β tetra- or pentapeptoids were efficiently obtained by macrocyclisation of the corresponding linear peptoids. In vitro competition binding experiments using [125I]-somatostatin were performed on this first generation of peptoids mimicking the SRIF pharmacophore (Phe7-(D)Trp8-Lys9-Thr10). The selectivity profiles of cyclic compounds 1 to 4 were similar with higher affinity for the sst3, sst5 and sst4 receptors and lower potency on sst1 and sst2 subtypes.

Published
2012

20. Expedient Solution-Phase Synthesis and NMR Studies of Arylopeptoids

Author

Sophie Faure, Thomas Hjelmgaard, Dan Staerk, John Nielsen, and Claude Taillefumier

Subjects
chemistry.chemical_classification, Peptidomimetic, Stereochemistry, Organic Chemistry, Peptide, Coupling reagent, chemistry.chemical_compound, chemistry, Side chain, Peptide bond, Physical and Theoretical Chemistry, Benzamide, Amide bonds, Solution phase synthesis
Abstract

The development of a highly convenient and efficient protocol for iterative solution-phase synthesis of shorter oligomers of para- and meta-arylopeptoids is described. Peptide coupling methods for accessing longer oligomers were studied: use of the new coupling reagent COMU was found to be the most efficient for creation of the tertiary benzamide bonds. The cis/trans isomerism of arylopeptoid backbones was studied by NMR and was found to be highly dependent on the nature of the side chains. Increasing bulkiness of theside chains favored the cis amide bond conformation; arylopeptoids possessing tert-butyl side chains contained exclusively cis amide bonds.

Published
2011

21. Convenient Solution-Phase Synthesis and Conformational Studies of Novel Linear and Cyclic α,β-Alternating Peptoids

Author

Claude Taillefumier, Thomas Hjelmgaard, Sophie Faure, Alison A. Edwards, Emiliana De Santis, and Cécile Caumes

Subjects
Molecular Structure, Protein Conformation, 010405 organic chemistry, Peptidomimetic, Chemistry, Stereochemistry, Molecular Sequence Data, Static Electricity, Organic Chemistry, Peptoid, 010402 general chemistry, Peptides, Cyclic, 01 natural sciences, Biochemistry, Combinatorial chemistry, 0104 chemical sciences, Peptoids, chemistry.chemical_compound, Amino Acid Sequence, Physical and Theoretical Chemistry, Solution phase synthesis
Abstract

The synthesis of a novel family of peptidomimetics composed of linear and cyclic alpha,beta-alternating peptoids is described. Oligomers consisting of up to six peptoid residues (n = 1-3) were synthesized on large scale with use of an efficient iterative solution-phase method and longer oligomers (n = 4, 5) were obtained by the coupling of appropriately protected shorter oligomers. Preliminary conformational studies of these hybrid peptoids are reported.

Published
2009

23. Cyclic β-Peptoids

Author

Claude Taillefumier, Sophie Faure, Claude Didierjean, Vincent Théry, Olivier Roy, Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
[CHIM.ORGA]Chemical Sciences/Organic chemistry, Stereochemistry, Organic Chemistry, Stereoisomerism, Crystal structure, Ring (chemistry), Biochemistry, Combinatorial chemistry, chemistry.chemical_compound, Protein structure, Template, chemistry, Tetramer, Physical and Theoretical Chemistry, Quantum, Derivative (chemistry)
Abstract

The first synthesis of functionalized beta-peptoid macrocycles is reported. X-ray crystallographic structure of tetramer 9 reveals a C2-symmetrical derivative with unexpected all-cis-amide bonds and spatial disposition of the appendages toward the two opposite faces of the ring. Quantum calculations suggest that 9 is locked in this layout. These macrocycles constitute novel promising templates for multimeric ligation of biologically active ligands. The concept was exemplified by chemical decoration of tetramer 9 via "click" reactions.

Published
2008

24. Multivalent thioglycopeptoids via photoclick chemistry: potent affinities towards LecA and BC2L-A lectins

Author

Cécile Caumes, Bertrand Legeret, Anne Imberty, Sophie Faure, Claude Taillefumier, Emilie Gillon, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
Burkholderia cenocepacia, Stereochemistry, 010402 general chemistry, 01 natural sciences, Catalysis, Coupling reaction, Peptoids, Lectins, Materials Chemistry, Molecule, [CHIM]Chemical Sciences, Sulfhydryl Compounds, biology, Molecular Structure, 010405 organic chemistry, Chemistry, Metals and Alloys, General Chemistry, biology.organism_classification, Photochemical Processes, Affinities, Combinatorial chemistry, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Pseudomonas aeruginosa, Ceramics and Composites, Click chemistry, Click Chemistry
Abstract

International audience; Solution-phase synthesis of linear and cyclic β- and α,β-peptoids was coupled to photo-induced thiol–ene coupling reaction to readily access multivalent thioglycoclusters. A tetrameric cyclic β-peptoid scaffold displaying 1-thio-β-D-galactose or 1-thio-α-D-mannose has revealed by ITC experiments efficient binding potency for bacterial lectins LecA and BC2L-A, respectively.

Published
2015

25. Immobilization of proteases on chitosan for the development of films with antibiofilm properties

Author

Claude Taillefumier, Olivier Roy, Sophie Faure, Philippe Michaud, S. Badel, Thierry Bernardi, Cédric Delattre, Pierre-Henri Elchinger, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Pascal (IP), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Centre National de la Recherche Scientifique (CNRS), and BioFilm Control, Biopôle Clermont Limagne, Saint-Beauzire

Subjects
Proteases, Staphylococcus aureus, Immobilized enzyme, Bacillus amyloliquefaciens, medicine.medical_treatment, Bacterial adhesion, Microbial Sensitivity Tests, medicine.disease_cause, Biochemistry, Microbiology, chemistry.chemical_compound, Structural Biology, Polysaccharides, medicine, [CHIM]Chemical Sciences, Bacillus licheniformis, Molecular Biology, Chitosan, Protease, biology, Pseudomonas aeruginosa, Biofilm, General Medicine, Fouling, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, Enzymes, Immobilized, Listeria monocytogenes, chemistry, Biofilms, Brain heart infusion, Peptide Hydrolases
Abstract

International audience; Bacterial resistance due to biofilm formation—particularly Staphylococci biofilms—is associated with multiple problems in medical settings where biofilms can colonize medical indwelling devices and cause nosocomial infections. It was against this backdrop that we explored the anti-biofilm activities of a set of proteases against biofilm formation by Staphylococcus aureus, Listeria monocytogenes and Pseudomonas aeruginosa. The selected screened enzymes were immobilized on chitosan to obtain films with anti-biofilm activities. Immobilization efficiency was about 94% for protease from Bacillus licheniformis and reached up to 96% for Neutrase. In vitro assays performed in brain heart infusion (BHI) broth using the Biofilm Ring Test highlighted that immobilized enzymes were efficient against biofilms of Staphylococci cultures, especially protease from B. licheniformis and Neutrase from Bacillus amyloliquefaciens.

Published
2015

26. ChemInform Abstract: From Glycopeptides to Glycopeptoids

Author

Sophie Faure, Thomas Szekely, Claude Taillefumier, and Olivier Roy

Subjects
chemistry.chemical_compound, chemistry, Stereochemistry, Amide, General Medicine, Oligomer, Glycopeptide
Abstract

This review covers the published literature describing the synthesis of glycopeptoids, a family of glycopeptide mimics. Members of this family are composed of an N-substituted glycine or β-alanine oligomer backbone linked to one or several carbohydrate moieties at the amide nitrogen atoms. The interest in this class of biomimetics lies in their enhanced proteolytic stability and greater conformational flexibility relative to glycopeptides. This Microreview not only describes the different methods for synthesising glycopeptoids but also discusses their application both as glycopeptidomimetics and glycocluster constructs.

Published
2014

28. Oxetane cis- and trans-β-amino-acid scaffolds from l-rhamnose by efficient SN2 reactions in oxetane rings; pseudoenantiomeric analogues of the antibiotic oxetin

Author

Stephen Johnson, John H. Jones, Sarah F. Jenkinson, George W. J. Fleet, Claude Taillefumier, and Donald Angus

Subjects
Rhamnose, Stereochemistry, Organic Chemistry, Oxetane, Catalysis, law.invention, Inorganic Chemistry, chemistry.chemical_compound, chemistry, Nucleophile, law, SN2 reaction, Azide, Physical and Theoretical Chemistry, Walden inversion, Trifluoromethanesulfonate, Cis–trans isomerism
Abstract

An efficient multigram ring contraction of a 1,4-lactone 2-O-triflate derived from l-rhamnose - with retention of configuration in the ring closure - is the key step in the preparation of a series of oxetanes, which are pseudoenantiomeric analogues of the naturally occurring antibiotic oxetin, an oxetane cis-β-amino acid. Subsequent nucleophilic displacements of the corresponding triflates by azide proceed in consistently excellent yields, without any elimination, to provide syntheses of scaffolds for analogues of the antibiotic. © 2004 Elsevier Ltd. All rights reserved.

Published
2004

29. Anomeric spiroannelated 1,4-diazepine 2,5-diones from furano exo-glycals: towards a new class of spironucleosides

Author

Yves Chapleur, Sabine Thielges, and Claude Taillefumier

Subjects
chemistry.chemical_compound, Diazepine, Anomer, Peptidomimetic, Chemistry, Stereochemistry, Organic Chemistry, Drug Discovery, Molecule, Stereoselectivity, Biochemistry
Abstract

The first synthesis of 1,4-diazepine 2,5-dione peptides containing a β-amino acid in which the β carbon is also the anomeric carbon of a furanoid sugar is described. These new anomeric spirosugars obtained with a stereoselective control in the d - gulo , d - manno , d - allo and d - ribo series can be regarded as the first members of a new class of spironucleosides. In the course of our study, two symmetrical tetrameric cyclopeptides comprising two identical sugar β-amino acid and α-amino acid residues were also isolated, these structures could be of interest as new potential host molecules.

Published
2004

30. Facile synthesis of fused furanosyl β-amino acids from protected sugar lactones: incorporation into a peptide chain

Author

Younes Lakhrissi, Yves Chapleur, Claude Taillefumier, and Mohammed Lakhrissi

Subjects
chemistry.chemical_classification, Anomer, Chemistry, Stereochemistry, Organic Chemistry, Peptide, Sequence (biology), Catalysis, Amino acid, Inorganic Chemistry, chemistry.chemical_compound, Benzylamine, Wittig reaction, Organic chemistry, Physical and Theoretical Chemistry, Sugar
Abstract

The synthesis of fused furanosyl β-amino esters from protected sugar lactones is described, using the combination of a Wittig type reaction and 1,4-addition of benzylamine on the resulting glycosylidenes. This sequence of reactions afford either N-glycosyl-3-ulosonic acid esters, which are the β-analogues of anomeric sugar α-amino esters, or open-chain sugar β-enamino esters, when a retro-Michael reaction takes place after addition of benzylamine. Incorporation of the fused furanosyl β-amino ester 2a into a peptide chain is also described.

Published
2002

31. Effect of proteases against biofilms of Staphylococcus aureus and Staphylococcus epidermidis

Author

Cédric Delattre, Thierry Bernardi, S. Badel, Pierre-Henri Elchinger, Sophie Faure, Claude Taillefumier, Olivier Roy, Philippe Michaud, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Institut Pascal (IP), SIGMA Clermont (SIGMA Clermont)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), BioFilm Control, and SIGMA Clermont (SIGMA Clermont)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])

Subjects
Proteases, Staphylococcus aureus, fouling, medicine.medical_treatment, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, medicine.disease_cause, Applied Microbiology and Biotechnology, Microbiology, Antibiotic resistance, Staphylococcus epidermidis, Endopeptidases, medicine, anti-biofilm, Subtilisins, Aspergillus, Protease, biology, Biofilm, Metalloendopeptidases, protease, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, 3. Good health, Anti-Bacterial Agents, Biofilms, Staphylococcus, Peptide Hydrolases
Abstract

UNLABELLED Biofilms play a key role in bacterial resistance against antibacterial agents-an issue that causes multiple problems in medical fields, particularly with Staphylococcus biofilms that colonize medical indwelling devices. The literature reports several anti-biofilm strategies that have been applied in medicine. Disrupting the biofilm formation process creates new sites open to colonization by treatment-generated planktonic bacteria, so efforts have turned to focus on strategies to prevent and control the initial Staphylococci adhesion. Here, we investigated the preventive activities of three commercial proteases (Flavourzyme, Neutrase and Alcalase) against biofilm formation by two Staphylococcus strains. Some proteolytic extracts revealed interesting results with Staphylococcus epidermidis and Staphylococcus aureus aureus biofilms. SIGNIFICANCE AND IMPACT OF THE STUDY Three proteases were tested against Staphylococcus aureus and Staphylococcus epidermidis biofilms in standard conditions. The Flavourzyme containing a mix of Aspergillus orizae endo- and exoproteases demonstrated significant efficacy against Staph. epidermidis biofilm formation. These results could prove valuable in the effort to develop simple anti-biofilm methods.

Published
2014

32. Macrocyclic arylopeptoids - a novel type of cyclic N-alkylated aromatic oligoamides forming nanotubular assemblies

Author

Olivier Roy, Sophie Faure, Thomas Hjelmgaard, Claude Taillefumier, D. Avignant, Claude Didierjean, Malika El-Ghozzi, Lionel Nauton, Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], and University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)

Subjects
Macrocyclic Compounds, Magnetic Resonance Spectroscopy, Nanostructure, Chemistry, Stereochemistry, Metals and Alloys, General Chemistry, Nuclear magnetic resonance spectroscopy, Alkylation, Combinatorial chemistry, Catalysis, Nanostructures, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Peptoids, X-Ray Diffraction, Benzamides, X-ray crystallography, Materials Chemistry, Ceramics and Composites, [CHIM]Chemical Sciences
Abstract

International audience; he head-to-tail conversion of linear arylopeptoids (oligomeric N-substituted aminomethyl benzamides) into the derived novel macrocycles has enabled the first X-ray structures of arylopeptoid constructs and the identification of well-defined architectures in solution.

Published
2014

33. Rapid and convenient semi-automated microwave assisted solid-phase synthesis of arylopeptoids

Author

Jakob E. Rasmussen, Sophie Faure, Claude Taillefumier, Thomas Hjelmgaard, John Nielsen, Marcello Massimo Boccia, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), University of Copenhage, Faculty of Health and Medical Sciences, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)

Subjects
Steric effects, Solid-phase synthesis, 010405 organic chemistry, Chemistry, Aromatic oligoamides, Organic Chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Combinatorial chemistry, Microwave assisted, 0104 chemical sciences, Microwave-assisted synthesis, Automated synthesis, Drug Discovery, Side chain, [CHIM]Chemical Sciences, Submonomer synthesis
Abstract

International audience; A facile and expedient route to the synthesis of arylopeptoid oligomers (N-alkylated aminomethyl benz-amides) using semi-automated microwave-assisted solid-phase synthesis is presented. The synthesis was optimized for the incorporation of side chains derived from sterically hindered or unreactive amines and both ortho- and para-substituted arylo-backbones. By utilizing this optimized protocol a complex nonameric arylopeptoid was synthesized in less than 11 h, featuring a novel alternating ortho-, meta-, and para-substituted backbone pattern and a variety of chemically diverse and challenging side chains.

Published
2014

34. Facile dibromoolefination of lactones using bromomethylenetriphenylphosphorane

Author

Françoise Chrétien, Younes Lakhrissi, Yves Chapleur, and Claude Taillefumier

Subjects
chemistry.chemical_compound, chemistry, Bromide, Methylenetriphenylphosphorane, Organic Chemistry, Drug Discovery, Organic chemistry, Halogenation, Biochemistry, Tetrahydrofuran
Abstract

Dibromoolefination of lactones was achieved in high yields using bromomethylenetriphenylphosphorane in refluxing tetrahydrofuran. This reaction is believed to proceed via bromination of the monobromophosphorane from the corresponding bromomethyltriphenylphosphonium bromide with concomitant formation of methylenetriphenylphosphorane as shown by 31P NMR. Transylidation should occur to afford the reactive dibromomethylenetriphenylphosphorane.

Published
2001

35. cis- and trans-3-Azido-oxetane-2-carboxylate scaffolds: hexamers of oxetane cis-β-amino acids

Author

Mark P. Watterson, Michael R. Probert, George W. J. Fleet, Donald Angus, Claude Taillefumier, Timothy D. W. Claridge, David J. Watkin, Sarah F. Barker, and Natasha L. Hungerford

Subjects
chemistry.chemical_classification, Stereochemistry, Organic Chemistry, Crystal structure, Oxetane, Biochemistry, Amino acid, chemistry.chemical_compound, chemistry, Nucleophile, Drug Discovery, Azide, Carboxylate, Cis–trans isomerism
Abstract

Efficient synthesis of both cis- and trans-3-azido-oxetane-2-carboxylates relies upon efficient nucleophilic displacements of 3-O-triflates of oxetanes by trifluoroacetate and azide. Such structures are scaffolds for incorporation of oxetane-β-amino acids into oligomers; the synthesis of a series of protected β-hexapeptides and the X-ray crystal structure of methyl 2,4-anhydro-6-deoxy-5-O-benzyl-L-altronate are reported. © 2001 Elsevier Science Ltd.

Published
2001

36. Enantiomerically pure decalinic structures from carbohydrates using intramolecular Diels-Alder and Ferrier carbocyclization

Author

Yves Chapleur and Claude Taillefumier

Subjects
Ferrier carbocyclization, Stereochemistry, Chemistry, Intramolecular force, Organic Chemistry, Diels alder, Organic chemistry, General Chemistry, Catalysis
Abstract

The synthesis of enantiomerically pure decalinic structures, advanced intermediates for the synthesis of the hexahydronaphtalen part of mevinic acids, is described. The key steps are the intramolecular Diels-Alder cycloaddition of a suitably substituted sugar enone obtained via the Ferrier rearrangement of tri-O-acetyl-D-glucal with the appropriate alcohol representing the diene part of the system. Chemical manipulation of the resulting, diastereomerically pure, cycloadduct led to a 5,6-unsaturated carbohydrate which was submitted to the Ferrier carbocylization. This reaction proved difficult likely because of the embedding of the aglycon in a cycle, the hydration product of the double bond being the main product. This compound was in turn transformed into the decalinic structures by treatment in basic medium. The inverse strategy, Ferrier carbocyclization followed by IMDA of an enone and a diene linked via an ester bond was unsuccessful.Key words: Intramolecular Diels-Alder reaction, enantiomerically pure decalin, Ferrier carbocyclization, carbohydrates.

Published
2000

37. Efficient conditions for the synthesis of C-glycosylidene derivatives: a direct and stereoselective route to C-glycosyl compounds

Author

Younes Lakhrissi, M. Lakhrissi, Claude Taillefumier, and Yves Chapleur

Subjects
chemistry.chemical_classification, Anomer, Chemistry, Organic Chemistry, Glycoside, Catalysis, Inorganic Chemistry, chemistry.chemical_compound, Microwave heating, Wittig reaction, Organic chemistry, Glycosyl, Stereoselectivity, Physical and Theoretical Chemistry
Abstract

Efficient conditions for the synthesis of C -glycosylidene compounds from lactones based on Wittig reactions of cyanomethyl triphenylphosphoranylidene involving microwave heating are described: subsequent stereoselective reduction of the anomeric olefins gave the corresponding C -glycosides in good yields with high stereocontrol.

Published
2000

38. Synthesis and biological testings as inhibitors of HMGCoA reductase of the seco-acid of tuckolide and its C-7 epimer

Author

Yves Chapleur, Stéphane Colle, Claude Taillefumier, Rex Liebl, and Arthur L. Schmidt

Subjects
Stereochemistry, Clinical Biochemistry, Drug Evaluation, Preclinical, Organophosphonates, Pharmaceutical Science, Biochemistry, Chemical synthesis, Gluconolactone, Butyric acid, Lactones, Magnoliopsida, Structure-Activity Relationship, chemistry.chemical_compound, Drug Discovery, Animals, Organic chemistry, Molecular Biology, Cells, Cultured, Aldehydes, biology, Organic Chemistry, Stereoisomerism, Plants, Hydroxymethylglutaryl-CoA reductase, Rats, chemistry, Enzyme inhibitor, Microsomes, Liver, biology.protein, Molecular Medicine, Hydroxymethylglutaryl CoA Reductases, Stereoselectivity, Epimer, Hydroxymethylglutaryl-CoA Reductase Inhibitors, Enone
Abstract

The seco-acid of the natural macrolactone, tuckolide (decarestrictin D) and the C-7 epimer have been prepared in enantiomerically pure form from d -gluconolactone and poly(3-hydroxy butyric acid). The key steps are Horner–Emmons olefination and stereoselective reduction of the resulting enone to provide both epimers at C-7. None of the seco-acids inhibit microsomal HMGCoA reductase of pea or rat liver. It may be concluded that the cholesterol biosynthesis inhibiting effect of tuckolide is unlikely to proceed via HMGCoA reductase inhibition.

Published
1999

40. Wittig olefination of partially protected sugar lactones: A direct entry to dioxabicyclic and trioxatricyclic systems

Author

C. Didierjean, M. Lakhrissi, Yves Chapleur, André Aubry, A. Chaouch, and Claude Taillefumier

Subjects
chemistry.chemical_compound, Direct entry, Bicyclic molecule, Chemistry, Furan, Organic Chemistry, Drug Discovery, Wittig reaction, Organic chemistry, Sugar, Biochemistry, Adduct
Abstract

Partially protected sugar lactones reacts with stabilized phosphoranes at high temperature yielding activated olefins which undergo subsequent 1,4-addition to give bicyclic adducts, simultaneous furan formation being also observed.

Published
1998

42. The tert-Butyl Side Chain: A Powerful Means to Lock Peptoid Amide Bonds in the Cis Conformation

Author

Claude Taillefumier, Sophie Faure, Cécile Caumes, Claude Didierjean, Yannick J. Esvan, Olivier Roy, Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), SIGMA Clermont (SIGMA Clermont)-Centre National de la Recherche Scientifique (CNRS)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Steric effects, Stereochemistry, Glycine, Molecular Conformation, Stereoisomerism, Crystallography, X-Ray, 010402 general chemistry, 01 natural sciences, Biochemistry, Molecular conformation, Peptoids, chemistry.chemical_compound, Amide, Side chain, [CHIM.CRIS]Chemical Sciences/Cristallography, Physical and Theoretical Chemistry, Amide bonds, Tert butyl, 010405 organic chemistry, Chemistry, Organic Chemistry, Peptoid, Amides, 0104 chemical sciences, 3. Good health, Oligopeptides
Abstract

International audience; The very simple sterically hindered tert-butyl side chain exerts complete control over the peptoid amide geometry which only exists in the cis conformation. It is exemplified in NtBu glycine homo-oligomers and in linear oligopeptoids designed with an alternating cis-trans backbone amide pattern.

Published
2013

43. α-Peptoïdes et composés apparentés : synthèse et contrôle de la conformation

Author

Cécile Caumes, Olivier Roy, Claude Taillefumier, Thomas Szekely, Sophie Faure, Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC), Imagerie intégrative de la molécule à l'organisme, and Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
α-Peptoïdes, 010405 organic chemistry, General Chemical Engineering, [SHS.ANTHRO-BIO]Humanities and Social Sciences/Biological anthropology, General Chemistry, 010402 general chemistry, 01 natural sciences, ComputingMilieux_MISCELLANEOUS, 0104 chemical sciences
Abstract

Resume Le squelette des peptoides derive de celui des peptides par deplacement des chaines laterales des carbones Cα vers les azotes d’amide. Ce principe a ete applique aux β-peptides pour conduire aux β-peptoides et recemment d’autres architectures de type peptoide, telles que les α,β-peptoides, arylopeptoides et N-hydroxy/alcoxy-peptoides ont ete rapportees dans la litterature. Cette revue dresse un bilan sur les peptoides et les nouvelles familles de composes apparentees, tant du point de vue de leur synthese que de leur preference conformationnelle. Une mise au point bibliographique est egalement apportee sur les recentes avancees en termes de controle de la geometrie cis/trans des amides N,N-disubstitues des peptoides.

Published
2013

44. Cyclic alpha,Beta-Tetrapeptoids: Sequence-Dependent Cyclization and Conformational Preference

Author

Carlos Fernandes, Thomas Hjelmgaard, Olivier Roy, Cécile Caumes, Sophie Faure, Claude Didierjean, Emmanuel Wenger, Claude Taillefumier, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), and Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, Stereochemistry, Molecular Conformation, Sequence (biology), Crystal structure, Crystallography, X-Ray, 010402 general chemistry, 01 natural sciences, Biochemistry, Peptoids, chemistry.chemical_compound, Sequence dependent, Amide, Side chain, [CHIM]Chemical Sciences, Amino Acid Sequence, Physical and Theoretical Chemistry, 010405 organic chemistry, Circular Dichroism, Organic Chemistry, 0104 chemical sciences, 3. Good health, chemistry, Cyclization, Oligopeptides
Abstract

International audience; The presence of at least one N-Cα branched side chain is crucial for successful cyclization of α,β-tetrapeptoids. The ctct amide sequence revealed in the crystal structure of the 14-membered cyclotetrapeptoid 8 is also the most populated conformation in solution and is reminiscent of the predominant amide arrangement of the 12-membered cyclic tetrapeptides (CTPs).

Published
2013

45. The click triazolium peptoid side chain: a strong cis-amide inducer enabling chemical diversity

Author

Olivier Roy, Sophie Faure, Cécile Caumes, Claude Taillefumier, Institut de Chimie de Clermont-Ferrand (ICCF), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Synthèse et étude de systèmes à intêret biologique (SEESIB), and Centre National de la Recherche Scientifique (CNRS)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP)

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, Stereochemistry, Peptidomimetic, 010402 general chemistry, 01 natural sciences, Biochemistry, Catalysis, Protein Structure, Secondary, chemistry.chemical_compound, Peptoids, Colloid and Surface Chemistry, Isomerism, Amide, Side chain, 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Peptoid, General Chemistry, Nuclear magnetic resonance spectroscopy, Triazoles, Antibonding molecular orbital, Amides, 0104 chemical sciences, chemistry, Two-dimensional nuclear magnetic resonance spectroscopy, Natural bond orbital
Abstract

International audience; Access to homogeneous and discrete folded peptoid structures primarily depends on control of the cis/trans isomerism of backbone tertiary amides. This can be achieved by designing specific side chains capable of forming local interactions with the backbone. This is often undertaken at the expense of side-chain diversity, which is a key advantage of peptoids over other families of peptidomimetics. We report for the first time a positively charged triazolium-type side chain that does not compromise diversity and exhibits the best ability reported to date for inducing the cis conformation. The cis-directing effect was studied in N-acetamide dipeptoid model systems and evaluated in terms of K(cis/trans) using NMR spectroscopy in aprotic and protic solvents. Computational geometry optimization and natural bond orbital analysis in combination with NOESY experiments were consistent with a model in which n → π*(Ar) electronic delocalization [from carbonyl (O(i-1)) to the antibonding orbital (π*) of the triazolium motif on residue i] may be operative. In the computational model (gas-phase) and experimentally in CDCl(3), H-bonding between the triazolium C-H proton and the C(i)═O(i) oxygen was also identified and may act cooperatively with the n → π*(Ar) delocalization, resulting in the absence of the trans rotamers in CDCl(3).

Published
2012

46. Improved solid-phase synthesis and study of arylopeptoids with conformation-directing side chains

Author

Thomas Hjelmgaard, Sophie Faure, Emiliana de Santis, Dan Staerk, Alexander, Bruce D., Edwards, Alison A., Claude Taillefumier, John Nielsen, Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Medway School of Pharmacy, Universities of Kent and Greenwich at Medway, School of Science, University of Greenwich, University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), and Bonnefoy, Stéphanie

Subjects
Foldamers Aromatic oligoamides Peptoids Solid-phase synthesis Conformational analysis
Abstract

International audience; The development of an improved methodology for iterative solid-phase synthesis of para- and metaarylopeptoids (oligomeric N-substituted aminomethyl benzamides) using benzoyl chloride building blocks is described. This methodology has enabled the synthesis of arylopeptoids with tert-butyl and phenyl side chains, which allows for complete control over the amide conformation: the tert-butyl results in a 100% cis amide conformation while the phenyl side chain results in a 100% trans amide conformation. The method has furthermore enabled the first synthesis and preliminary conformational studies of arylopeptoids bearing (S)-N-(1-phenylethyl) side chains.

Published
2012

47. Synthesis and binding affinities for sst receptors of cyclic peptoid SRIF-mimetics

Author

Cécile Caumes, Thomas Hjelmgaard, Olivier Roy, Morgane Reynaud, Denis Servent, Claude Taillefumier, Sophie Faure, Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Bonnefoy, Stéphanie

Abstract

International audience; Mimicking the tetradecapeptide somatostatin through the design of novel non-peptide small molecules is needed for developing analogues with selective or universal affinity for human somatostatin receptors (hsst1-5) and improved pharmacological properties. We report the synthesis and evaluation of the binding potential of the first all-peptoid SRIF (somatotropin release-inhibiting factor) analogues. Cyclic β and mixed α/β tetra- or pentapeptoids were efficiently obtained by macrocyclisation of the corresponding linear peptoids. In vitro competition binding experiments using [125I]-somatostatin were performed on this first generation of peptoids mimicking the SRIF pharmacophore (Phe7-(D)Trp8-Lys9-Thr10). The selectivity profiles of cyclic compounds 1 to 4 were similar with higher affinity for the sst3, sst5 and sst4 receptors and lower potency on sst1 and sst2 subtypes.

Published
2012

48. Effect of capping groups at the N- and C-termini on the conformational preference of ?,?-peptoids

Author

Claude Taillefumier, Giuliano Siligardi, Alison A. Edwards, Emiliana De Santis, Bruce D. Alexander, Sophie Faure, Cécile Caumes, Thomas Hjelmgaard, Simon J. Holder, Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Protein Folding, Spectrophotometry, Infrared, Chemistry, Peptidomimetic, Stereochemistry, Circular Dichroism, Organic Chemistry, Proteolytic enzymes, Peptoid, Biochemistry, Protein Structure, Secondary, chemistry.chemical_compound, Residue (chemistry), Peptoids, Intramolecular force, Amide, Side chain, [CHIM]Chemical Sciences, Physical and Theoretical Chemistry, Dimerization, Cis–trans isomerism
Abstract

Peptoids (N-substituted glycines, i.e. a-peptoids) are artificial oligoamides which are closely related structurally to a-peptides with the side chains located on the amide nitrogen rather than the a-carbon (Fig. 1). A major advantage of a-peptoids is their ease of synthesis, particularly by the so-called ‘submonomer method’. A further benefit is the vast potential for diversity as the side chains on the amide nitrogens are introduced by primary amines. Therefore a-peptoids are particularly well suited for the construction of peptidomimetic libraries in the context of drug discovery as they have been shown to be resistant to proteolytic enzymes. Peptoids occupy a unique position as peptidomimetic foldamers since their backbones are deprived of free NH amides and thus have decreased capacity to form intramolecular H-bonding interactions. Although unnatural, a peptoid residue is structurally related to a proline as the coupling of residues gives tertiary amide bonds which can populate cis and trans conformations. These features confer greater flexibility to oligopeptoids but interestingly they maintain the propensity to form ordered secondary structures. a-Peptoids containing aromatic or aliphatic a-chiral side chains can fold into stable helical structures. For example, homo-peptoids with (S)-1-cyclohexylethyl or (S)-1-naphthylethyl side chains (s1npe) were reported to adopt, both in the solid

Published
2012

49. Efficient and versatile COMU-mediated solid-phase submonomer synthesis of arylopeptoids (oligomeric N-substituted aminomethyl benzamides)

Author

John Nielsen, Claude Taillefumier, Thomas Hjelmgaard, Sophie Faure, Dan Staerk, Department of Basic Sciences and Environment, Department of Chemistry [Copenhagen], Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
chemistry.chemical_classification, Molecular Structure, Chemistry, Morpholines, Organic Chemistry, Salt (chemistry), Stereoisomerism, Chemistry Techniques, Synthetic, Amides, Biochemistry, Peptoids, chemistry.chemical_compound, Phase (matter), Reagent, Oximes, [CHIM]Chemical Sciences, Organic chemistry, Physical and Theoretical Chemistry, Acids, Benzoic acid
Abstract

International audience; The development of a highly efficient methodology for solid-phase synthesis of para- and meta-arylopeptoids (oligomeric N-substituted aminomethyl benzamides) with free acids or free amides at the C-terminus is described. The arylopeptoids were synthesised by means of a convenient submonomer protocol in which the arylopeptoid residues were created in an iterative manner on the growing chain using an acylation-substitution cycle. The uronium salt COMU was found to be the most efficient reagent for ensuring fast and clean couplings of the benzoic acid building blocks

Published
2011

50. Cyclic alpha, beta-peptoid octamers with differing side chain patterns: synthesis and conformational investigation

Author

Olivier Roy, Emiliana De Santis, Giuliano Siligardi, Rohanah Hussain, Claude Didierjean, Claude Taillefumier, Thomas Hjelmgaard, Bruce D. Alexander, Tamás Jávorfi, Sophie Faure, Alison A. Edwards, Synthèse et étude de systèmes à intêret biologique (SEESIB), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Circular dichroism, Magnetic Resonance Spectroscopy, Chemistry, Peptidomimetic, Stereochemistry, Organic Chemistry, Clinical Biochemistry, α, Molecular Conformation, Peptoid, Nuclear magnetic resonance spectroscopy, Crystal structure, Crystallography, X-Ray, Biochemistry, Crystallography, chemistry.chemical_compound, Peptoids, β-peptoids, X-ray crystallography, [CHIM.CRIS]Chemical Sciences/Cristallography, Side chain, Histone octamer, Peptidomimetics
Abstract

International audience; The solution-phase synthesis and cyclisation of three alpha,beta-peptoid octamers with differing side chain patterns is reported. One of these, compound C, showed a significantly greater resolution by NMR relative to the other two structurally related octamers. This observation was studied in detail by circular dichroism at a synchrotron light source to facilitate the correlation between the side chain patterns and conformational preference of these three peptoids. The X-ray crystal structure of cyclic octamer C, the first high-resolution structure for the α,β-peptoid backbone, was also obtained from methanol. Combined solid- and solution-phase studies allowed the identification of the N-2-(benzyloxy)ethyl side chain on the β-residue of the heterogeneous backbone as a key structural feature driving the increased conformational stability for octamer C

Published
2011

Catalog

Books, media, physical & digital resources
See catalog results