Serveur d'exploration sur le nickel au Maghreb

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The influence of aspartic or glutamic acid residues in tetrapeptides on the formation of complexes with nickel(II) and zinc(II)

Identifieur interne : 000474 ( France/Analysis ); précédent : 000473; suivant : 000475

The influence of aspartic or glutamic acid residues in tetrapeptides on the formation of complexes with nickel(II) and zinc(II)

Auteurs : H. Kozlowski [Pologne] ; A. Lebkiri [Maroc] ; Ch. O. Onindo [Royaume-Uni] ; L. D. Pettit [Royaume-Uni] ; J.-F. Galey [France]

Source :

RBID : ISTEX:4B3D4D86B2C1A6DC66C7EFEF3AA5C893DCFA6A83

Abstract

The formation of the complexes formed by NiII and ZnII with Asp-Asp-Asp and a series of tetrapeptides containing one or two Asp residues or one Glu residue are reported. Stability constants were measured pH-metrically. The particular species and the metal ion binding sites were determined using 1H NMR, UV-vis and CD spectroscopy. The β-carboxylate group of the Asp residue stabilizes the complexes significantly, particularly when present as the N-terminal residue. As a result the tendency for NiII to deprotonate and bind to amide-nitrogen atoms, forming planar diamagnetic complexes, is reduced and their formation delayed to a significantly higher pH when compared to other peptides. The side chain of the Glu residue has a much smaller effect. As anticipated, ZnII was unable to deprotonate and bind to peptide nitrogens.

Url:
DOI: 10.1016/0277-5387(94)00239-B


Affiliations:


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ISTEX:4B3D4D86B2C1A6DC66C7EFEF3AA5C893DCFA6A83

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