Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1249607 | Vibrational Spectroscopy | 2012 | 6 Pages |
Abstract
A series of solid tripeptides Boc-Gly-X-Gly-OMe (XÂ =Â dehydroalanine (ÎAla), dehydrophenylalanine (ÎPhe)) was investigated by Raman scattering and Fourier transform infrared spectra to examine the conformational marker bands of the unsaturated residue. The observed fundamental modes gave us the opportunity to analyze structural features that change due to the substitution of Ala by ÎAla and due to the different spatial arrangement of ÎPhe (Z and E isomers). In addition, we showed the alteration of the spectral profile when the large size residue (Phe) is introduced into the backbone of the peptide with ÎPhe (in Boc-Gly-Î(Z)Phe-Phe-OMe). The frequency ranges of interest included the NH stretching, carbonyl stretching, and amide deformation modes as well as vibrations of the investigated dehydroresidues. The observed differences of positions and intensities of IR and Raman bands provided an insight into the structural and spectroscopic properties of the selected dehydropeptides.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Kamilla Malek, Maciej Makowski,