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

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;: