Sanna, Daniele and Agoston, Csaba Gábor and Micera, Giovanni and Sóvágó, Imre (2001) The Effect of the ring size of fused chelates on the thermodynamic and spectroscopic properties of peptide complexes of copper(II). Polyhedron, Vol. 20 (26-27), p. 3079-3090. ISSN 0277-5387. Article.
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Copper(II) complexes of the tripeptides GlyGly-β-Ala, Gly-β-AlaGly, β-AlaGlyGly, Gly-β-Ala-β-Ala, β-AlaGly-β-Ala, β-Ala-β-Ala-β-Ala and the tetrapeptides GlyGlyGly-β-Ala, GlyGly-β-AlaGly, Gly-β-AlaGlyGly and β-AlaGlyGlyGly were studied by potentiometric, EPR and UV-Vis spectroscopic methods. The stoichiometry of the complexes of peptides containing β-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 all cases. The presence of -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 β-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.
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