The impact of the amino-acid sequence on the specificity of copper[II] interactions with peptides having nonco-ordinating side-chains

• Autorzy: Bal W. , Dyba M. , Kozlowski H.
• Języki publikacji: EN

Abstrakty

EN

The review presents specific interactions that occur in complexes of Cu(ll) 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(ll) 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.

Słowa kluczowe

EN

stability constant; peptide; interaction; copper; amino acid

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1997
• Tom: 44
• Numer: 3
• Opis fizyczny: p.467-476,fig.

Twórcy

autor

Bal W.

• University of Wroclaw, F.Joliot-Curie 14, 50-383 Wroclaw, Poland

autor

Dyba M.

autor

Kozlowski H.

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