Copper(II) complexes of the tripeptides GlyGly-beta -Ala, Gly-beta -AlaGly, beta -AlaGlyGly, Gly-beta -Ala-beta -Ala, beta -AlaGly-beta -Ala, beta -Ala-beta -Ala-beta -Ala and the tetrapeptides GlyGlyGly-beta -Ala, GlyGly-beta -AlaGly, Gly-beta -AlaGlyGly and beta -AlaGlyGlyGly were studied by potentiometric, EPR and UV-Vis spectroscopic methods. The stoichiometry of the complexes of peptides containing P-alanine residues are very similar to those of oligoglycines; [CuL](+), [CuL2], [CuH-1L], [CuH-2L](-), [CuH-1L2](-) and [CuH-3L](2-) were detected as the major species in ail cases. The presence of beta -alanine residues, however, influenced both thermodynamic stability and coordination geometry of various complexes. In most cases the formation of six-membered chelate rings resulted in a decrease of thermodynamic stability and distortion of coordination geometry of peptide complexes, especially if beta -alanine residues were present in N-terminal or adjacent positions. On the contrary, the formation of the mixed (5,6,5) and (5,5,6) linked chelate systems of tripeptides is favoured over the pure five-membered rings. (C) 2001 Elsevier Science Ltd. All rights reserved.

The effect of the ring size of fused chelates on the thermodynamic and spectroscopic properties of peptide complexes of copper(II) / Sanna, D; Agoston, Cg; Micera, Giovanni; Sovago, I.. - In: POLYHEDRON. - ISSN 0277-5387. - 20:26-27(2001), pp. 3079-3090. [10.1016/S0277-5387(01)00918-4]

The effect of the ring size of fused chelates on the thermodynamic and spectroscopic properties of peptide complexes of copper(II)

MICERA, Giovanni;
2001

Abstract

Copper(II) complexes of the tripeptides GlyGly-beta -Ala, Gly-beta -AlaGly, beta -AlaGlyGly, Gly-beta -Ala-beta -Ala, beta -AlaGly-beta -Ala, beta -Ala-beta -Ala-beta -Ala and the tetrapeptides GlyGlyGly-beta -Ala, GlyGly-beta -AlaGly, Gly-beta -AlaGlyGly and beta -AlaGlyGlyGly were studied by potentiometric, EPR and UV-Vis spectroscopic methods. The stoichiometry of the complexes of peptides containing P-alanine residues are very similar to those of oligoglycines; [CuL](+), [CuL2], [CuH-1L], [CuH-2L](-), [CuH-1L2](-) and [CuH-3L](2-) were detected as the major species in ail cases. The presence of beta -alanine residues, however, influenced both thermodynamic stability and coordination geometry of various complexes. In most cases the formation of six-membered chelate rings resulted in a decrease of thermodynamic stability and distortion of coordination geometry of peptide complexes, especially if beta -alanine residues were present in N-terminal or adjacent positions. On the contrary, the formation of the mixed (5,6,5) and (5,5,6) linked chelate systems of tripeptides is favoured over the pure five-membered rings. (C) 2001 Elsevier Science Ltd. All rights reserved.
The effect of the ring size of fused chelates on the thermodynamic and spectroscopic properties of peptide complexes of copper(II) / Sanna, D; Agoston, Cg; Micera, Giovanni; Sovago, I.. - In: POLYHEDRON. - ISSN 0277-5387. - 20:26-27(2001), pp. 3079-3090. [10.1016/S0277-5387(01)00918-4]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/48900
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