Copper(II) complexes of peptides containing two or three histidyl residues (Ac-HisGlyHis-OH, Ac-HisGlyHis-NHMe, Ac-HisHisGlyHis-OH and Ac-HisHisGlyHis-NHMe) have been studied by potentiometric, UV-Vis, EPR and CD spectroscopic measurements. The imidazole nitrogen atoms are described as the primary metal binding sites of all ligands resulting in the formation of various macrochelates in the pH range 4 to 7. The (N-im, N-, N-im)-co-ordinated [CuH-1L](0(+)) complexes were mainly detected in samples containing free carboxylates at the C-termini, whilst the [CuH-2L](-(0)) complexes were the predominant species in slightly alkaline solution and their binding modes were described via 4N-co-ordination (N-im, N-, N-, N-im) in (7,5,6)- membered fused chelate rings. Deprotonation and co-ordination of the third amide nitrogens were detected above pHsimilar to9 in all cases.
Copper(II) complexes of N-terminal protected tri- and tetrapeptides containing histidine residues / Sanna, D; Micera, Giovanni; Kallay, C; Rigo, V; Sovago, I.. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - 17(2004), pp. 2702-2707. [10.1039/b407909d]