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Start Over Author "Baptiste Legrand" Journal journal of medicinal chemistry
2 results on '"Baptiste Legrand"'

1. Mapping the N-Terminal Hexokinase-I Binding Site onto Voltage-Dependent Anion Channel-1 To Block Peripheral Nerve Demyelination

Author

Benoit Gautier, Mélanie Forêt Jacquard, Sophie Guelfi, Scarlette Abbou, Elisa Gonzalez, Jade Berthelot, Hassan Boukhaddaoui, Aurélien Lebrun, Baptiste Legrand, Nicolas Tricaud, and Nicolas Inguimbert

Subjects
Binding Sites, Hexokinase, Drug Discovery, Molecular Medicine, Humans, Peripheral Nervous System Diseases, Voltage-Dependent Anion Channels, Peripheral Nerves, Demyelinating Diseases
Abstract

The voltage-dependent anion channel (VDAC), the most abundant protein on the outer mitochondrial membrane, is implicated in ATP, ion and metabolite exchange with cell compartments. In particular, the VDAC participates in cytoplasmic and mitochondrial Ca

Published
2022

2. From a marine neuropeptide to antimicrobial pseudopeptides containing aza-β(3)-amino acids: structure and activity

Author

Joël Henry, Michèle Baudy-Floc’h, Arnaud Bondon, Baptiste Legrand, Céline Zatylny-Gaudin, Mathieu Laurencin, Emilie Duval, Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Structures et interactions moléculaires, Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Physiologie et Ecophysiologie des Mollusques Marins (PE2M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Centre National de la Recherche Scientifique (CNRS), We thank SERB Laboratories and Region Bretagne for their financial support., Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), and De Villemeur, Hervé

Subjects
Models, Molecular, Circular dichroism, MESH: Amino Acids, Magnetic Resonance Spectroscopy, Molecular Conformation, MESH: Rabbits, MESH: Cricetinae, Peptide, MESH: Neuropeptides, 01 natural sciences, MESH: Gram-Positive Bacteria, MESH: Circular Dichroism, MESH: Structure-Activity Relationship, MESH: Cricetulus, Cricetinae, MESH: Gram-Negative Bacteria, Drug Discovery, MESH: Animals, Amino Acids, chemistry.chemical_classification, MESH: Microbial Sensitivity Tests, Oligopeptide, Chemistry, Circular Dichroism, MESH: Antimicrobial Cationic Peptides, Stereoisomerism, Nuclear magnetic resonance spectroscopy, [SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences, MESH: Hemolysis, Amino acid, Anti-Bacterial Agents, [SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, MESH: Oligopeptides, Molecular Medicine, Rabbits, Oligopeptides, MESH: Models, Molecular, Stereochemistry, [SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, CHO Cells, Microbial Sensitivity Tests, 010402 general chemistry, Gram-Positive Bacteria, Hemolysis, Article, Turn (biochemistry), Structure-Activity Relationship, Cricetulus, MESH: CHO Cells, MESH: Anti-Bacterial Agents, Gram-Negative Bacteria, Structure–activity relationship, Animals, MESH: Molecular Conformation, Aza Compounds, MESH: Magnetic Resonance Spectroscopy, 010405 organic chemistry, Neuropeptides, MESH: Stereoisomerism, 0104 chemical sciences, MESH: Aza Compounds, Antimicrobial Cationic Peptides
Abstract

Incorporation of aza-β3-amino acids into endogenous neuropeptide from mollusks (ALSGDAFLRF-NH2) with weak antimicrobial activities allows us to design new AMPs sequences. We find that, depending on the nature of the substitution, these could result either in inactive pseudopeptides or in a drastic enhancement of the antimicrobial activity without high cytotoxicity resulted. Structural studies perform by NMR and circular dichroism on the pseudopeptides show the impact of aza-β3-amino acids on the peptide structures. We obtain the first three-dimensional structures of pseudopeptides containing aza-β3-amino acids in aqueous micellar SDS and demonstrate that hydrazino turn can be formed in aqueous solution. Overall, these results demonstrate the ability to modulate AMPs activities through structural modifications induced by the nature and the position of these amino acid analogs in the peptide sequences.

Published
2012

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