The influence of aspartic or glutamic acid residues in tetrapeptides on the formation of complexes with nickel(II) and zinc(II)
Identifieur interne : 000C03 ( Istex/Curation ); précédent : 000C02; suivant : 000C04The 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 :
- Polyhedron [ 0277-5387 ] ; 1995.
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
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Galey</name><affiliation wicri:level="1"><mods:affiliation>Chimie Macromoléculaire, Université de Lille I, 59655 Villeneuve d'Ascq, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Chimie Macromoléculaire, Université de Lille I, 59655 Villeneuve d'Ascq</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Polyhedron</title><title level="j" type="abbrev">POLY</title><idno type="ISSN">0277-5387</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">14</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="211">211</biblScope><biblScope unit="page" to="218">218</biblScope></imprint><idno type="ISSN">0277-5387</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0277-5387</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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