Impact of α,β-dehydroamino acid residues on the binding abilities of di-, tri- and tetra-peptides

Abstract

Insertion of a dehydroamino acid residue into a sequence of di-, tri- or tetra-peptide changed considerably the binding abilities of peptide ligands towards copper(II) ions. Potentiometric and spectroscopic (EPR, UV-VIS and CD) data have shown that the amide nitrogen of the dehydroamino acid residue is more effective in co-ordination than its parent analogue. In the case of the bulky ΔPhe residue also the (Z–E) isomerisation has a critical impact on the co-ordination equilibria in the system studied.