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Self‐organization Properties of a GPCR‐Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy

Abstract : Conjugation of the bioactive apelin‐17 peptide with a fluorocarbon chain results in self‐organization of the peptide into micelles. Fluorine NMR spectroscopy studies show that the fluoropeptide‘s micelles are monodisperse, 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 which enables the number of molecules present in the micelle to be estimated as 200, in agreement with values found by dynamic light scattering measurements.
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https://hal.archives-ouvertes.fr/hal-03090942
Contributor : Marc-André DELSUC Connect in order to contact the contributor
Submitted on : Sunday, October 10, 2021 - 5:29:24 PM
Last modification on : Sunday, June 26, 2022 - 3:15:38 AM

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Capucine Jourdain de Muison, Sridevi M. Ramanoudjame, Lucie Esteoulle, Claude Ling, Germain Brou, et al.. Self‐organization Properties of a GPCR‐Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy. ChemBioChem, 2020, 22 (4), pp.657-661. ⟨10.1002/cbic.202000601⟩. ⟨hal-03090942⟩

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