The Ac–RGD–NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO

• DOI: 10.1002/bip.10335
• Publication Date: 2003-04-22T10:01:40Z
• Authors: Nikolaos Biris; Athanassios Stavr...; Anastasia S. Politou; Emmanuel Mikros; Maria Sakarellos‐...; Constantinos Saka...; Vassilios Tsikaris
• Keywords: Cyclic peptide; Peptide fragment

Abstract According to general belief, the conformational information on short linear peptides in solution derived at ambient temperature from NMR spectrometry represents a population‐weighted average over all members of an ensemble rapidly interconverting conformations. Usually search for discrete conformations is concentrated low temperatures especially when sharp resonances are detected room temperature. Using peptide Ac–RGD–NH 2 (Ac–Arg–Gly–Asp–NH , Ac: acetyl) as model system and following new approach, we have been able demonstrate that can adopt states DMSO‐ d 6 (DMSO: dimethylsulfoxide) which vary way critically dependent reconstitution conditions used before their dissolution . The conformers stabilized by intramolecular hydrogen bonds, persist high undergo very slow exchange with extended structures chemical shift time scale. reported findings provide clear evidence occurrence solvent‐induced point DMSO valuable medium folding studies peptides. © 2003 Wiley Periodicals, Inc. Biopolymers 69:72–86,