IR investigation on dehydrophenylalanine containing model peptides in helical conformation deposited on a crystal...

Fourier transform ir spectra have been recorded for three 3(10)-helical and one alpha-helical pentapeptides containing dehydrophenylalanine, in a thin solid film, in order to find marker bands for various secondary structures encountered in peptides containing dehydroaminoacids. The peptide solutions were deposited and dried as thin film on zinc selenide crystal surface. This convenient sampling method has provided reliable estimates of peptide secondary structure in solid state. Detailed vibrational assignments in the spectral region between 1200-1700 cm(-1) are reported. In this region, peptide amide I, II, and III vibrations occur. Spectra-structure correlation has been presented based on the amide modes. Comparison of the ir spectra with available crystal structure data provides qualitative support for assignments of ir bands to 3(10)-helical structure and alpha-helical structure in dehydrophenylalanine containing pentapeptides. Band frequency assignments for 3(10)-helical conformation are consistent for all three peptides. All the assignments agree closely with the theoretical predictions. The spectral differences between 3(10)-helical peptides and the alpha-helical peptide have been highlighted. These findings demonstrate that a method based on ir spectroscopy can be developed for a useful approximation of three-dimensional structure of dehydropeptides in solid state. Copyright 1999 John Wiley & Sons, Inc.