Sóvágó Imre, Osz Katalin
Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4010, Debrecen, Hungary.
Dalton Trans. 2006 Aug 28(32):3841-54. doi: 10.1039/b607515k. Epub 2006 Jul 17.
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 NH2-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.
本文综述了肽的金属结合亲和力和选择性，特别强调了肽复合物的高度结构多样性。这些复合物最常见的结构类型是由相邻酰胺基团以稠合五元螯合环的形式去质子化并与金属离子配位形成的。详细讨论了该过程的金属离子选择性以及各种锚定基团的作用。肽的最高金属结合亲和力与两个锚定基团在适当位置的存在（“双锚”）有关：例如NH2-Xaa-Xaa-His/Cys/Asp/Met-Xaa序列。在侧链供体功能中，组氨酸残基的咪唑和半胱氨酸残基的硫醇盐是最有效的配位基团，它们参与金属结合会导致形成多种不同的大环螯合物或环结构和/或各种多核配合物。已经对这些结构基序的实例及其可能的应用进行了深入讨论。
