Influence of solvents on conformation of dehydropeptides

Structural investigations of dehydropeptides containing (Z)-dehydrophenylalanine in solvents characterized by different polarity are discussed. The conformational analysis are based on spectroscopic methods (NMR, CD), molecular modeling techniques and in case of the tripeptide, ab initio methods. The results of temperature experiment indicate, that the only conformation of the investigated hexapeptide 3 is stabilized by intramolecular hydrogen bonds. Depending on the length of the peptide chain, the polarity of solvent influences on arrangement of the side chain of the amino acids or of the main chain of the peptide.