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Dalton Transactions

The international journal for inorganic, organometallic and bioinorganic chemistry



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Dalton Trans., 2008, 4978 - 4980, DOI: 10.1039/b807799a

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

Justyna Brasu, Marek Cebrat, Aleksandra Sochacka, Olimpia Gadysz and Jolanta witek-Kozowska

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.

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