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 special sequences of non-bonding side-chains. Unusual coordination modes resulting from the introduction of the break-point proline residues are also discussed. The second part of the review describes the binding properties of histidine peptides. The effects of the positioning of a His residue are discussed in the terms of cooperation and competition between potential metal anchoring sites. Special attention is given to His-3 peptides, modeling the biologically relevant albumin-like metal binding site. Finally, the coordination-related specific hydrolysis processes in histidine peptides are briefly discussed. (C) 1999 Elsevier Science S.A. All rights reserved.