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• W2949417966 abstract "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." @default.
• W2949417966 created "2019-06-27" @default.
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• W2949417966 date "1997-09-30" @default.
• W2949417966 modified "2023-10-17" @default.
• W2949417966 title "The impact of the amino-acid sequence on the specificity of copper(II) interactions with peptides having nonco-ordinating side-chains." @default.
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• W2949417966 doi "https://doi.org/10.18388/abp.1997_4397" @default.
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