VCD studies on cyclic peptides assembled from L-α-amino acids and a trans-2-aminocyclopentane- or trans-2-aminocyclohexane carboxylic acid

E. Vass, U. Strijowski, K. Wollschläger, I. M. Mándity, G. Szilvágyi, M. Jewgiński, K. Gaus, S. Royo, Z. Majer, N. Sewald, M. Hollósi

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The increasing interest in peptidomimetics of biological relevance prompted us to synthesize a series of cyclic peptides comprising trans-2-aminocyclohexane carboxylic acid (Achc) or trans-2-aminocyclopentane carboxylic acid (Acpc). NMR experiments in combination with MD calculations were performed to investigate the three-dimensional structure of the cyclic peptides. These data were compared to the conformational information obtained by electronic circular dichroism (ECD) and vibrational circular dichroism (VCD) spectroscopy. Experimental VCD spectra were compared to theoretical VCD spectra computed quantum chemically at B3LYP/6-31G(d) density functional theory (DFT) level. The good agreement between the structural features derived from the VCD spectra and the NMR-based structures underlines the applicability of VCD in studying the conformation of small cyclic peptides.

Original languageEnglish
Pages (from-to)613-620
Number of pages8
JournalJournal of Peptide Science
Volume16
Issue number11
DOIs
Publication statusPublished - Nov 1 2010

Keywords

  • Cyclic peptides
  • Electronic circular dichroism
  • NMR
  • Vibrational circular dichroism
  • trans-2-aminocyclohexane carboxylic acid
  • trans-2-aminocyclopentane carboxylic acid

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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