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9 results on '"Ludovic T. Maillard"'

1. Tailoring the Physicochemical Properties of Antimicrobial Peptides onto a Thiazole-Based γ-Peptide Foldamer

Author

Nicolas Masurier, Agnès Masnou, Clément Bonnel, Estelle Jumas-Bilak, Young Kee Kang, Ludovic T. Maillard, Patricia Licznar-Fajardo, Matthieu Simon, Baptiste Legrand, Margaux Clavié, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Hydrosciences Montpellier (HSM), Institut national des sciences de l'Univers (INSU - CNRS)-Institut de Recherche pour le Développement (IRD)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), CHU Montpellier, Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier), and Chungbuk National University

Subjects
Erythrocytes, Antimicrobial peptides, Peptide, Microbial Sensitivity Tests, Gram-Positive Bacteria, 01 natural sciences, Hemolysis, 03 medical and health sciences, chemistry.chemical_compound, Drug Discovery, Amphiphile, Gram-Negative Bacteria, Side chain, Molecule, Humans, [CHIM]Chemical Sciences, Thiazole, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Foldamer, Fungi, Metabolic stability, Combinatorial chemistry, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, 0104 chemical sciences, Anti-Bacterial Agents, 010404 medicinal & biomolecular chemistry, Thiazoles, chemistry, Drug Design, Molecular Medicine, Antimicrobial Cationic Peptides
Abstract

Antimicrobial peptides (AMPs) are amphipathic molecules displaying broad-spectrum bactericidal activity, providing opportunities to develop a new generation of antibiotics. However, their use is limited either by poor metabolic stability or by high hemolytic activity. We herein addressed the potential of thiazole-based γ-peptide oligomers named ATCs as tunable scaffolds to design polycationic AMP mimetics. Knowing the side chain distribution along the backbone, we rationally designed facially amphiphilic sequences with bactericidal effect in the micromolar range. Since no hemolytic activity was detected up to 100 μM, this class of compounds has shown the potential for therapeutic development.

Published
2020

2. Topological Requirements for CI-M6PR-Mediated Cell Uptake

Author

Julie Aguesseau-Kondrotas, Marcel Garcia, Alain Morère, Anastasia Godefroy, Ludovic T. Maillard, Magali Gary-Bobo, Lamiaa M. A. Ali, Matthieu Simon, Christophe Nguyen, Khaled El Cheikh, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), and NanoMedSyn

Subjects
Models, Molecular, Glycoconjugate, Protein Conformation, media_common.quotation_subject, [SDV]Life Sciences [q-bio], Cell, Biomedical Engineering, Pharmaceutical Science, Bioengineering, 02 engineering and technology, Topology, 01 natural sciences, Receptor, IGF Type 2, Protein structure, Cell Line, Tumor, medicine, Humans, [CHIM]Chemical Sciences, Internalization, Receptor, media_common, Pharmacology, chemistry.chemical_classification, 010405 organic chemistry, Chemistry, Ligand, Organic Chemistry, Biological Transport, 021001 nanoscience & nanotechnology, 0104 chemical sciences, medicine.anatomical_structure, Cell culture, 0210 nano-technology, Biotechnology
Abstract

International audience; The 300 kDa cation-independent M6P receptor (CI-MPR) mediates ligand internalization and trafficking to the endolysosomal compartments. Because of its endocytotic nature, it has been recognized as a promising class of receptors for target component delivery. Its cellular uptake involves the simultaneous binding of two protein units resulting in the formation of receptor dimers. While many multivalent glycoconjugates have been reported to date, little is known about the topological requests to induce an effective recruitment of CI-MPRs. We herein describe the synthesis and cell uptake ability of a set of highly organized glycoclusters bearing one to three saccharide units. The spatial arrangement of carbohydrate ligands is ensured by a heterocyclic γ-peptide central core.

Published
2019

3. C 9/12 Ribbon-Like Structures in Hybrid Peptides Alternating α- and Thiazole-Based γ-Amino Acids

Author

Jean-Louis Bantignies, Nicolas Masurier, Ludovic T. Maillard, Baptiste Legrand, Clément Bonnel, Young Kee Kang, Emmanuel Wenger, Matthieu Simon, François Hoh, Jean Martinez, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Charles Coulomb (L2C), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Chungbuk National University, Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institute of Organic Chemistry, Universität Zürich [Zürich] = University of Zurich (UZH), and Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)

Subjects
chemistry.chemical_classification, amino acids, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], 010405 organic chemistry, Stereochemistry, Hydrogen bond, Organic Chemistry, structure elucidation, General Chemistry, Nuclear magnetic resonance spectroscopy, 010402 general chemistry, 01 natural sciences, Catalysis, 0104 chemical sciences, Amino acid, torsion angles, ribbon structures, chemistry.chemical_compound, chemistry, Ribbon, peptides, Fourier transform infrared spectroscopy, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Thiazole
Abstract

International audience; According to their restricted conformational freedom, heterocyclic -amino acids are usually considered to be related to Z-vinylogous -amino acids. In this context, oligomers alternating -amino acids and thiazole-based -amino acids (ATCs) were expected to fold into a canonical 12-helical shape as described for /-hybrid peptides composed of cis-/-unsaturated -amino acids. However, through a combination of X-ray crystallography, NMR spectroscopy, FTIR experiments, and DFT calculations, it was determined that the folding behavior of ATC-containing hybrid peptides is much more complex. The homochiral /(S)-ATC sequences were unable to adopt a stable conformation, whereas the heterochiral /(R)-ATC peptides displayed novel ribbon structures stabilized by unusual C-9/12-bifurcated hydrogen bonds. These ribbon structures could be considered as a succession of pre-organized / dipeptides and may provide the basis for designing original -helix mimics.

Published
2017

4. 1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases

Author

Carine Bebrone, Jean Martinez, Jean-François Hernandez, Lionel Nauton, Laurent Gavara, Gülhan Turan-Zitouni, Filomena De Luca, Paola Sandra Mercuri, Ludovic T. Maillard, Jean Denis Docquier, Silvia Tanfoni, Moreno Galleni, Katja Becker, Pauline Lonjon, Jean-Marie Frère, Laurent Sevaille, Ciarán Condon, Carole Guyon, Maud E. S. Achard, Julia Dzieciolowski, Lionel Benard, Luisa Borgianni, Otto Dideberg, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université de Liège, Università degli Studi di Siena = University of Siena (UNISI), 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), Anadolu University, Justus-Liebig-Universität Gießen = Justus Liebig University (JLU), Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes (LBMCE), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Expression Génétique Microbienne (EGM (UMR_8261 / FRE_3630)), Institut de biologie physico-chimique (IBPC (FR_550)), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), 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), 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)-École Supérieure Chimie Physique Électronique de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Faculty of Pharmacy Department of Pharmaceutical Chemistry (ANADOLU UNIVERSITY), Justus-Liebig-Universität Gießen (JLU), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Institute of Organic Chemistry, Universität Zürich [Zürich] = University of Zurich (UZH), laboratoire de chimie et pharmacologie de molécules d'intérêt biologique, Service d'Hématologie, Laboratory for Biological Macromolecules [Liège, Belgium], Université de Liège-Center for Protein Engineering-Institut de Chimie B6 [Liège, Belgium], Dipartimento Biotecnol Med, University of Siena, Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Anadolu Üniversitesi, Eczacılık Fakültesi, Farmasötik Kimya Anabilim Dalı, and 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)

Subjects
0301 basic medicine, Lactams, Stereochemistry, Stenotrophomonas maltophilia, Metalloenzymes, MBL superfamily, 4-Triazole-3-thione, Biochemistry, beta-Lactamases, Nitrogen Heterocycles, Structure-Activity Relationship, 03 medical and health sciences, chemistry.chemical_compound, Antibiotics, Drug Discovery, Hydrolase, 1,2,4-Triazole-3-thione, Bacterial resistance, Metallo-β-Lactamase, β-Lactam antibiotic, Structure–activity relationship, [CHIM]Chemical Sciences, General Pharmacology, Toxicology and Pharmaceutics, Beta-Lactamase Inhibitors, ComputingMilieux_MISCELLANEOUS, Pharmacology, chemistry.chemical_classification, Dose-Response Relationship, Drug, Molecular Structure, biology, Bicyclic molecule, Aryl, Organic Chemistry, Thiones, Active site, Triazoles, bacterial infections and mycoses, biology.organism_classification, Aeromonas hydrophila, 3. Good health, 030104 developmental biology, Enzyme, chemistry, biology.protein, Molecular Medicine, beta-Lactamase Inhibitors, Bacterial Resistance, Bacteria
Abstract

52nd International Conference on Medicinal Chemistry (RICT) of the French-Medicinal-Chemistry-Society (SCT) - Interfacing Chemical Biology and Drug Discovery -- JUL 06-08, 2016 -- Caen, FRANCE, WOS: 000403905300014, PubMed ID: 28505394, Metallo-beta-lactamases (MBLs) cause resistance of Gram-negative bacteria to beta-lactam antibiotics and are of serious concern, because they can inactivate the last-resort carbapenems and because MBL inhibitors of clinical value are still lacking. We previously identified the original binding mode of 4-amino-2,4-dihydro-5-(2-methylphenyl)-3H-1,2,4-triazole-3-thione (compound IIIA) within the dizinc active site of the L1 MBL. Herein we present the crystallographic structure of a complex of L1 with the corresponding non-amino compound IIIB (1,2-dihydro-5-(2-methylphenyl)-3H-1,2,4-triazole-3-thione). Unexpectedly, the binding mode of IIIB was similar but reverse to that of IIIA. The 3D structures suggested that the triazolethione scaffold was suitable to bind to the catalytic site of dizinc metalloenzymes. On the basis of these results, we synthesized 54 analogues of IIIA or IIIB. Nineteen showed IC50 values in the micromolar range toward at least one of five representative MBLs (i.e., L1, VIM-4, VIM-2, NDM-1, and IMP-1). Five of these exhibited a significant inhibition of at least four enzymes, including NDM-1, VIM2, and IMP-1. Active compounds mainly featured either halogen or bulky bicyclic aryl substituents. Finally, some compounds were also tested on several microbial dinuclear zinc-dependent hydrolases belonging to the MBL-fold superfamily (i.e., endonucleases and glyoxalase II) to explore their activity toward structurally similar but functionally distinct enzymes. Whereas the bacterial tRNases were not inhibited, the best IC50 values toward plasmodial glyoxalase II were in the 10 mm range., French Med Chem Soc, Univ Caen, Agence Nationale de la Recherche ("ANTIMBL") [ANR-14-CE16-0028-01]; Deutsche Forschungsgemeinschaft [BE1540/15-2 within SPP 1710]; Agence Nationale de la Recherche [ANR-06-BLAN-0086], We thank Mr. Pierre Sanchez for mass spectrometry analyses and Wolfram Meyer-Klaucke for advice about tRNase Z. Part of this work was supported by the Agence Nationale de la Recherche ("ANTIMBL", ANR-14-CE16-0028-01, including a fellowship to L.S.), the Deutsche Forschungsgemeinschaft (BE1540/15-2 within SPP 1710 to K.B.), and Agence Nationale de la Recherche ("subtilRNA", ANR-06-BLAN-0086) to C.C.

Published
2017

5. FT-​IR and NMR structural markers for thiazole-​based γ-​peptide foldamers

Author

Nicolas Masurier, Ludovic T. Maillard, Jean Martinez, Jean-Louis Bantignies, Baptiste Legrand, Clément Bonnel, Hugo Petitjean, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Laboratoire Charles Coulomb (L2C), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM ICMMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut de Chimie du CNRS (INC), and ANR-15-CE07-0004,CatFold,Criblage de l'activité catalytique de gamma-peptides autoorganisés(2015)

Subjects
Models, Molecular, Protein Conformation, alpha-Helical, Protein Folding, Magnetic Resonance Spectroscopy, Peptidomimetic, Stereochemistry, Nuclear magnetic resonance spectroscopy of nucleic acids, 010402 general chemistry, 01 natural sciences, Biochemistry, Oligomer, chemistry.chemical_compound, Protein structure, Spectroscopy, Fourier Transform Infrared, Physical and Theoretical Chemistry, Thiazole, 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Organic Chemistry, Foldamer, Hydrogen Bonding, Nuclear magnetic resonance spectroscopy, 3. Good health, 0104 chemical sciences, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Thiazoles, chemistry, Protein folding, Peptidomimetics, Peptides
Abstract

Nuclear magnetic resonance (NMR) spectroscopy has been established as a potent method for the determination of foldamer structures in solution. However, the NMR techniques could be limited by averaging, so additional experimental techniques are often needed to fully endorse the folding properties of a sequence. We have recently demonstrated that oligo-γ-peptides composed of 4-amino(methyl)-1,3-thiazole-5-carboxylic acids (ATCs) adopt an original helical fold stabilized by hydrogen bonds forming C9 pseudocycles. The main objective of the present work is to reinvestigate the folding of ATC oligomer 1 in order to identify reliable FT-IR and NMR structural markers that are of value for tracking the degree of organization of ATC-based peptides.

Published
2016

6. Thiazole-Based γ-Building Blocks as Reverse-Turn Mimetic to Design a Gramicidin S Analogue: Conformational and Biological Evaluation

Author

Séverine Zirah, Vincent Lisowski, Jean Martinez, Baptiste Legrand, Loïc Mathieu, Ludovic T. Maillard, Soahary Andriamanarivo, Young Kee Kang, Nicolas Masurier, Aurélien Lebrun, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Molécules de Communication et Adaptation des Micro-organismes (MCAM), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), and Chungbuk National University

Subjects
Circular dichroism, Magnetic Resonance Spectroscopy, Stereochemistry, Molecular Conformation, Gramicidin S, Molecular Dynamics Simulation, 010402 general chemistry, Antiparallel (biochemistry), Gram-Positive Bacteria, 01 natural sciences, Catalysis, Protein Structure, Secondary, chemistry.chemical_compound, Gram-Negative Bacteria, Amino Acid Sequence, Amino Acids, Thiazole, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, Tetrapeptide, 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Circular Dichroism, Organic Chemistry, Gramicidin, General Chemistry, Nuclear magnetic resonance spectroscopy, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, 0104 chemical sciences, Amino acid, Anti-Bacterial Agents, Thiazoles, chemistry, Drug Design, Antibacterial activity, Oligopeptides
Abstract

This paper describes the ability of a new class of heterocyclic γ-amino acids named ATCs (4-amino(methyl)-1,3-thiazole-5-carboxylic acids) to induce turns when included in a tetrapeptide template. Both hybrid Ac-Val-(R or S)-ATC-Ile-Ala-NH2 sequences were synthesized and their conformations were studied by circular dichroism, NMR spectroscopy, MD simulations, and DFT calculations. It was demonstrated that the ATCs induced highly stable C9 pseudocycles in both compounds promoting a twist turn and a reverse turn conformation depending on their absolute configurations. As a proof of concept, a bioactive analogue of gramicidin S was successfully designed using an ATC building block as a turn inducer. The NMR solution structure of the analogue adopted an antiparallel β-pleated sheet conformation similar to that of the natural compound. The hybrid α,γ-cyclopeptide exhibited significant reduced haemotoxicity compared to gramicidin S, while maintaining strong antibacterial activity.

Published
2014

7. Imidazopyridine-fused [1,3]-diazepinones: Synthesis and antiproliferative activity

Author

Marcel Garcia, Ophélie Vaillant, Dominique P. Arama, Joëlle Dubois, Ludovic T. Maillard, Jean Martinez, Audrey Gallud, Vincent Lisowski, Marie Maynadier, Nicolas Masurier, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Institut de Chimie des Substances Naturelles (ICSN), and Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
Imidazopyridine, Pyridines, Cell, Antineoplastic Agents, chemistry.chemical_compound, Cell Line, Tumor, Neoplasms, Drug Discovery, medicine, Cytotoxic T cell, Humans, Cell Proliferation, Pharmacology, Chemistry, Kinase, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Melanoma, Organic Chemistry, General Medicine, Azepines, medicine.disease, 3. Good health, medicine.anatomical_structure, Biochemistry, Cell culture, Hepatocyte, Cancer research, Growth inhibition, Drug Screening Assays, Antitumor
Abstract

International audience; : A series of 15 pyrido-imidazo-1,3-diazepin-5-ones and pyrido-1,3-diazepine-2,5-diones were synthesized and their anticancer activities were evaluated. Among tested compounds on a cell lines panel, compound 6a presents the best growth inhibition activity on 21 cell lines with a cytotoxic effect on MDA-MB-435 melanoma cells. This compound led to deep cell morphological changes and revealed to be an inhibitor of the Hepatocyte progenitor kinase-like kinase (HGK), which is known to be implicated in the migration, adhesion and invasion of various tumor cells.

Published
2014

8. A tandem aza-Friedel-Crafts reaction/Hantzsch cyclization: a simple procedure to access polysubstituted 2-amino-1,3-thiazoles

Author

Jean Martinez, Nicolas Masurier, Guilhem Chaubet, Ludovic T. Maillard, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), and Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)

Subjects
2-a]pyridine, Tandem, Hantzsch cyclization, 010405 organic chemistry, Chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Organic Chemistry, 2-Amino-1, 010402 general chemistry, 01 natural sciences, Biochemistry, 0104 chemical sciences, chemistry.chemical_compound, Thiourea, Simple (abstract algebra), Drug Discovery, Organic chemistry, 3-thiazoles, Friedel–Crafts reaction, aza-FriedeleCrafts reaction, Imidazo[1
Abstract

International audience; A tandem aza-FriedeleCrafts reaction/Hantzsch cyclization is described to access various polysubstituted 2-amino-1,3-thiazoles from electron-rich (hetero)-aromatic rings, aldehydes, thiourea and a-chloroketones.

Published
2011

9. Fluorous tagged N-hydroxy phthalimide for the parallel synthesis of O-aryloxyamines

Author

Florence S. Gaucher-Wieczorek, Philippe Durand, Ludovic T. Maillard, Bernard Badet, Institut de Chimie des Substances Naturelles (ICSN), and Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
Hydrocarbons, Fluorinated, Molecular Structure, 010405 organic chemistry, Aryl, Phthalimides, Stereoisomerism, General Chemistry, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, 010402 general chemistry, Boronic Acids, 01 natural sciences, Combinatorial chemistry, Catalysis, 0104 chemical sciences, Phthalimide, chemistry.chemical_compound, Aminolysis, chemistry, Combinatorial Chemistry Techniques, Organic chemistry, Amines, Copper
Abstract

International audience; The parallel synthesis of O-aryloxyamines remains an unfulfilled need in the field of medicinal chemistry and fragment-based approaches. To fill this gap a solution-phase two-step process based on (1) a copper-catalyzed cross-coupling of aryl boronic acids with a fluorous tagged N-hydroxyphthalimide, and (2) a supported aminolysis was designed and optimized using Taguchi's method. A library of O-aryloxyamines was synthesized in high yields with high purity and diversity.

Published
2010

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