11 Papers
205 Citations
Loïc Martin is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Synaptobrevin & Endopeptidase activity. The author has an hindex of 5, co-authored 11 publications. Previous affiliations of Loïc Martin include Council for the Curriculum, Examinations & Assessment.
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Papers
Cooperative exosite-dependent cleavage of synaptobrevin by tetanus toxin light chain.
Fabrice Cornille,Loïc Martin,Christine Lenoir,Didier Cussac,Bernard P. Roques,Marie-Claude Fournie-Zaluski +5 more
TL;DR: Results favor an exosite-controlled hydrolysis of synaptobrevin by TeNT, probably involving a conformational change of the toxin, which could account for the high degree of substrate specificity of TeNT and, probably, botulinum neurotoxins.
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Metallopeptidase inhibitors of tetanus toxin: A combinatorial approach.
Loïc Martin,Fabrice Cornille,Serge Turcaud,Hervé Meudal,Bernard P. Roques,Marie-Claude Fournie-Zaluski +5 more
TL;DR: Combinatorial libraries of pseudotripeptides, containing an ethylene sulfonamide or an m-sulfonamidophenyl moiety as the P1 side chain and natural amino acids in P1 and P2' positions, were synthesized and the best inhibitory activity was observed with Tyr and His as P1' and P 2' components, respectively.
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A Sensitive and Rapid Fluorescence-Based Assay for Determination of Tetanus Toxin Peptidase Activity
J M Soleilhac,Fabrice Cornille,Loïc Martin,Christine Lenoir,Marie-Claude Fournie-Zaluski,Bernard P. Roques +5 more
TL;DR: This novel enzymatic assay, which could be easily extended to other clostridial neurotoxins, is a major improvement in term of sensitivity and time saving, compared to currently used methods (SDS-PAGE, HPLC).
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β-Amino-thiols inhibit the zinc metallopeptidase activity of tetanus toxin light chain
TL;DR: A beta-amino-(4-sulfamoylphenyl)glycine-thiol, the first significantly efficient inhibitor of tetanus neurotoxin with a Ki value of 35 +/- 5 microM is designed.
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