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VCD studies on cyclic peptides assembled from L ‐α‐amino acids and a trans ‐2‐aminocyclopentane‐ or trans ‐2‐aminocyclohexane carboxylic acid
Author(s) -
Vass E.,
Strijowski U.,
Wollschläger K.,
Mándity I. M.,
Szilvágyi G.,
Jewgiński M.,
Gaus K.,
Royo S.,
Majer Z.,
Sewald N.,
Hollósi M.
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1272
Subject(s) - vibrational circular dichroism , peptidomimetic , chemistry , density functional theory , circular dichroism , carboxylic acid , cyclic peptide , peptide , stereochemistry , computational chemistry , organic chemistry , biochemistry
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. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.