The infrared and Raman spectra of solid tridehydropeptides : influence of ΔAla and ΔPhe on the spectral profile
author:
Małek Kamilla , Makowski Maciej
journal title:
Vibrational Spectroscopy
title of volume:
Selected Papers from the 6th International Conference on Advanced Vibrational Spectroscopy (ICAVS-6) and Two-Dimensional Correlation Spectroscopy (2DCOS-6) Sonoma County, CA, USA, 9–17th June 2011
A series of solid tripeptides Boc-Gly-X-Gly-OMe (X = dehydroalanine (
Ala), dehydrophenylalanine
(
Phe)) 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
Ala and due
to the different spatial arrangement of
Phe (
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
Phe (in Boc-Gly-
(Z)
Phe-Phe-OMe). The frequency ranges of interest included the NH stretching, car-
bonyl 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
keywords in English:
Dehydroalanine, Tripeptides, Dehydrophenylalanine, IR, Raman