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Issue 37, 2008
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The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+

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Abstract

A new vasopressin analogue, [His1,6]AVP, was synthesized and characterized by potentiometric measurements as well as by UV-Vis, CD and EPR spectroscopy. At the physiological pH the peptide forms a stable complex with Cu2+ ions which is characterized by the {NH2, NIm, NIm(macrochelate)} binding mode. The replacement of both Cys by His residues in the vasopressin sequence results in a very significant increase in the efficiency of Cu2+ binding.

Graphical abstract: The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+

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Publication details

The article was received on 08 May 2008, accepted on 08 Jul 2008 and first published on 06 Aug 2008


Article type: Communication
DOI: 10.1039/B807799A
Dalton Trans., 2008, 4978-4980

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    The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+

    J. Brasuń, M. Cebrat, A. Sochacka, O. Gładysz and J. Świątek-Kozłowska, Dalton Trans., 2008, 4978
    DOI: 10.1039/B807799A

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