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 journalArticle

10 Citations (Scopus)

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 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
JournalBiopolymers
Volume69
Issue number1
DOIs
StatePublished - May 2003
Externally publishedYes

Fingerprint

Dimethyl Sulfoxide
Peptides
Nuclear magnetic resonance
Temperature
Conformations
Chemical shift
Spectrometry
Hydrogen bonds
Dissolution
Hydrogen
Spectrum Analysis
arginyl-glycyl-aspartic acid
Population

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

Biris, N., Stavrakoudis, A., Politou, A. S., Mikros, E., Sakarellos-Daitsiotis, M., Sakarellos, C., & Tsikaris, V. (2003). The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO. Biopolymers, 69(1), 72-86. https://doi.org/10.1002/bip.10335

The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO. / Biris, Nikolaos; Stavrakoudis, Athanassios; Politou, Anastasia S.; Mikros, Emmanuel; Sakarellos-Daitsiotis, Maria; Sakarellos, Constantinos; Tsikaris, Vassilios.

In: Biopolymers, Vol. 69, No. 1, 05.2003, p. 72-86.

Research output: Contribution to journalArticle

Biris, N, Stavrakoudis, A, Politou, AS, Mikros, E, Sakarellos-Daitsiotis, M, Sakarellos, C & Tsikaris, V 2003, 'The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO', Biopolymers, vol. 69, no. 1, pp. 72-86. https://doi.org/10.1002/bip.10335
Biris N, Stavrakoudis A, Politou AS, Mikros E, Sakarellos-Daitsiotis M, Sakarellos C et al. The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO. Biopolymers. 2003 May;69(1):72-86. https://doi.org/10.1002/bip.10335
Biris, Nikolaos ; Stavrakoudis, Athanassios ; Politou, Anastasia S. ; Mikros, Emmanuel ; Sakarellos-Daitsiotis, Maria ; Sakarellos, Constantinos ; Tsikaris, Vassilios. / The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO. In: Biopolymers. 2003 ; Vol. 69, No. 1. pp. 72-86.
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