Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue European Biophysics Journal Année : 2007

Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface.

Résumé

Cateslytin (bCGA (344)RSMRLSFRARGYGFR(358)), a five positively charged 15 amino-acid residues arginine-rich antimicrobial peptide, was synthesized using a very efficient procedure leading to high yields and to a 99% purity as determined by HPLC and mass spectrometry. Circular dichroism, polarized attenuated total reflectance fourier transformed infrared, polarization modulation infrared reflection Absorption spectroscopies and proton two-dimensional NMR revealed the flexibility of such a peptide. Whereas being mostly disordered as a dry powder or in water solution, the peptide acquires a alpha-helical character in the "membrane mimicking" solvent trifuoroethanol. In zwitterionic micelles of dodecylphophatidylcholine the helical character is retained but to a lesser extent, the peptide returning mainly to its disordered state. A beta-sheet contribution of almost 100% is detected at the air-water interface. Such conformational plasticity is discussed regarding the antimicrobial action of Cateslytin.

Domaines

Chimie organique

Dates et versions

hal-00689903 , version 1 (20-04-2012)

Identifiants

Citer

Frantz Jean-François, Lucie Khemtémourian, Benoît Odaert, Sabine Castano, Axelle Grélard, et al.. Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface.. European Biophysics Journal, 2007, 36 ((8)), pp.1019-27. ⟨10.1007/s00249-007-0169-8⟩. ⟨hal-00689903⟩
56 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More