Metal ion selectivity of oligopeptides

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157 Citations (Scopus)

Abstract

Metal binding affinity and selectivity of peptides are reviewed with a special emphasis on the high structural variety of peptide complexes. The most common structural type of these complexes is built up by the deprotonation and metal ion coordination of subsequent amide groups in the form of fused five-membered chelate rings. The metal ion selectivity of this process and the role of various anchoring groups are discussed in detail. The highest metal binding affinity of peptides is connected to the presence of two anchoring groups in appropriate location (the "double anchor"): e.g. the NH 2-Xaa-Xaa-His/Cys/Asp/Met-Xaa sequence. Among the side chain donor functions, the imidazole of histidyl and thiolate of cysteinyl residues are the most effective ligating groups and their involvement in metal binding results in a great variety of different macrochelate or loop structures and/or formation of various polynuclear complexes. Examples of these structural motifs and their possible applications have been thoroughly discussed.

Original languageEnglish
Pages (from-to)3841-3854
Number of pages14
JournalDalton Transactions
Issue number32
DOIs
Publication statusPublished - 2006

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Oligopeptides
Metal ions
Metals
Peptides
Deprotonation
Anchors
Amides

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Metal ion selectivity of oligopeptides. / Sóvágó, I.; Ősz, K.

In: Dalton Transactions, No. 32, 2006, p. 3841-3854.

Research output: Contribution to journalArticle

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