Specific structure-stability relations in metallopeptides

This review discusses the modes of coordination of oligopeptides by Cu(II) and Ni(II). Special attention is given to tno general classes of peptides. The first part of the review deals with indirect effects introduced by spec ial sequences of non-bonding side-chains. Unusual coordination modes result ing from the introduction of the break-point proline residues are also disc ussed. The second part of the review describes the binding properties of hi stidine peptides. The effects of the positioning of a His residue are discu ssed in the terms of cooperation and competition between potential metal an choring sites. Special attention is given to His-3 peptides, modeling the b iologically relevant albumin-like metal binding site. Finally, the coordina tion-related specific hydrolysis processes in histidine peptides are briefl y discussed. (C) 1999 Elsevier Science S.A. All rights reserved.