Issue 17, 2004

Copper(ii) complexes of N-terminal protected tri- and tetra-peptides containing histidine residues

Abstract

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 (Nim, N, Nim)-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 (Nim, N, N, Nim) in (7,5,6)-membered fused chelate rings. Deprotonation and co-ordination of the third amide nitrogens were detected above pH ∼9 in all cases.

Graphical abstract: Copper(ii) complexes of N-terminal protected tri- and tetra-peptides containing histidine residues

Article information

Article type
Paper
Submitted
26 May 2004
Accepted
12 Jul 2004
First published
09 Aug 2004

Dalton Trans., 2004, 2702-2707

Copper(II) complexes of N-terminal protected tri- and tetra-peptides containing histidine residues

D. Sanna, G. Micera, C. Kállay, V. Rigó and I. Sóvágó, Dalton Trans., 2004, 2702 DOI: 10.1039/B407909D

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