OPTICAL ROTATION STUDIES OF COPPER (II)-TRIPEPTIDE COMPLEXES

Abstract

Copper(II) complexes of various optically active di- and tripeptides have been studied with the aid of optical rotatory dispersion (ORD) and circular dichroism (CD) techniques. The magnitudes of the molecular rotations related to the d-d transitions of the complexes fall into three different ranges, depending on the positions of asymmetric carbon atoms of the ligands. The molecular rotations of GAG and GLG complexes are greater than those of GGA, GGL, and GGV complexes, which are again greater than those of AGG, LGG, and VGG complexes (G, A, L, and V are glycine, alanine, leucine, and valine residues, respectively, in the tripeptides investigated, the N-terminal residue being the first residue in each abbreviation). The structures of these complexes, deduced from their potentiometric equilibrium curves and from the known crystal structure of the copper(II)-triglycine complex, show that the asymmetric carbon atoms of the second and third amino acid residues (counting from the N-terminal amino acid residue) are in the plane composed of the central metal ion, the nitrogen atoms of the amino and peptide groups, and the oxygen atom of the carboxylate group. The magnitude of the Cotton effect increases with the planarity of the chelate rings which include the asymmetric carbon atom and the metal ion, and with increasing strength of the coordinate bonds that form these chelate rings. Further support for this interpretation is found in the CD spectra of the copper(II) and nickel(II) complexes of AGG, GAG, GGA, and AAA. Analysis of the CD spectra of LL and DL alanylalanine complexes also demonstrate the influence of planarity and coordinate bond strength on the magnitude of the Cotton effect. Schiff base formation of aldehydes and ketones with dialanines causes fundamental changes in the geometries of the copper(II) complexes and reverses the relative contributions of the chelate rings to the total CD absorption intensities of the complexes.