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

Nikolaos Biris, Athanassios Stavrakoudis, Anastasia S. Politou, Emmanuel Mikros, Maria Sakarellos-Daitsiotis, Constantinos Sakarellos, Vassilios Tsikaris

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


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 of rapidly interconverting conformations. Usually the search for discrete conformations is concentrated at low temperatures especially when sharp NMR resonances are detected at room temperature. Using the peptide Ac-RGD-NH2 (Ac-Arg-Gly-Asp-NH2, Ac: acetyl) as a model system and following a new approach, we have been able to demonstrate that short linear peptides can adopt discrete conformational states in DMSO-d6 (DMSO: dimethylsulfoxide) which vary in a way critically dependent on the reconstitution conditions used before their dissolution in DMSO-d6. The conformers are stabilized by intramolecular hydrogen bonds, which persist at high temperatures and undergo a very slow exchange with their extended structures in the NMR chemical shift time scale. The reported findings provide clear evidence for the occurrence of solvent-induced conformational exchange and point to DMSO as a valuable medium for folding studies of short linear peptides.

Original languageEnglish (US)
Pages (from-to)72-86
Number of pages15
Issue number1
StatePublished - May 1 2003


  • Arginine ionic interactions
  • Aspartic acid ionic interactions
  • Fibrinogen inhibitor
  • Hydrogen bonds
  • NMR
  • Peptide folding
  • RGD peptide
  • Slow conformational exchange

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry


Dive into the research topics of 'The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO'. Together they form a unique fingerprint.

Cite this