Co-oligopeptides of aromatic amino acids and glycine with a variable distance between the aromatic residues. VI. Circular dichroism studies of Co-oligopeptides of l-phenylalanine, L-tryptophan, and glycine.

The circular dichroic properties of H-Gly-Phe-(Gly)_n-Trp-Gly-OH (II, n = 0,1,2) and of related simpler peptides, such as H-Phe-Gly-OH, H-Gly-Phe-OH, H-Gly-Phe-Gly-OH, H-Phe-Trp-OH, H-Phe-Trp-Gly-OH, and H-Gly-Phe-Trp-OH in water and trifluoroethanol solutions are investigated. Peptides containing only one phenylalanyl residue show markedly different near-uv dichroic signals depending on whether this residue is in the N-terminal position or not. The possible origin of this feature is discussed. The study of the oligopeptides II (n = 0,1,2) shows that no strong intramolecular interaction between the two aromatic rings is present. However, the dichroic properties of II (n = 0) are clearly anomalous, and the analysis of H-Gly-Phe-Trp-OH, H-Phe-Trp-Gly-OH, and of H-Phe-Trp-OH at different pH's, confirms that the presence of two adjacent aromatic residues may bring about chiroptical properties which indicate a restriction in the conformational equilibrium of the molecule. The limits, and the possible generalization of this finding, are discussed.