Bal W, Dyba M, Kozłowski H
Faculty of Chemistry, University of Wrocław, Poland.
Acta Biochim Pol. 1997;44(3):467-76.
The review presents specific interactions that occur in complexes of Cu(II) ions with peptides composed only of amino acids with nonco-ordinating side chains. Three classes of such peptides are discussed. The first type (NSFRY analogues) is characterised by the presence of a specific combination of bulky and aromatic residues, leading to a formation of multiple weak interactions around Cu(II) that result in an extremely high stability of complexes. The second class is composed of complexes of vasopressins and oxytocins, achieving superstability through a pre-conformation in the peptide molecule. The third group are oligopeptides containing one or two proline residues. These peptides form exotic macrochelate loops with Cu(II) in a result of the break-point effect of Pro residues. Particular emphasis in the review was given to stability constants of complexes, compared to oligoglycine or oligoalanine peptides.
该综述介绍了铜（II）离子与仅由具有非配位侧链的氨基酸组成的肽形成的复合物中发生的特定相互作用。讨论了三类这样的肽。第一类（NSFRY类似物）的特征是存在大量和芳香族残基的特定组合，导致在铜（II）周围形成多个弱相互作用，从而使复合物具有极高的稳定性。第二类由加压素和催产素的复合物组成，通过肽分子中的预构象实现超稳定性。第三类是含有一个或两个脯氨酸残基的寡肽。由于脯氨酸残基的断点效应，这些肽与铜（II）形成奇特的大环螯合物环。与寡甘氨酸或寡丙氨酸肽相比，该综述特别强调了复合物的稳定常数。
