Self-organization properties of a GPCR binding peptide incorporating fluorinated tail studied by fluorine NMR.
Fiche publication
Date publication
septembre 2020
Journal
Chembiochem : a European journal of chemical biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KIEFFER Bruno, Dr DELSUC Marc-André, Mr LING Claude, Dr BONNET Dominique
Tous les auteurs :
Jourdain de Muizon C, Ramanoudjame S, Esteoulle L, Ling C, Brou G, Anton N, Vandamme T, Delsuc MA, Bonnet D, Kieffer B
Lien Pubmed
Résumé
The conjugation of the bioactive apelin-17 peptide with a fluorocarbon chain results in self-organisational property of the peptide into micelles. Fluorine NMR studies show that fluoropeptide's micelles are mono-disperse while proton NMR indicates that the peptide moiety remains largely disordered despite micellization. A very fast exchange rate is measured between the free and micellar states of the peptide enabling to estimate the number of molecules present in the micelle as two hundred, in agreement with values found by Dynamic Light Scattering measurements.
Mots clés
Fluorine NMR GPCR ligand Micellization apelin- 17 peptide
Référence
Chembiochem. 2020 Sep 28;: