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

Justyna Brasuń; Marek Cebrat; Aleksandra Sochacka; Olimpia Gładysz; Jolanta Świątek-Kozłowska

doi:10.1039/B807799A

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Dalton Transactions

Issue 37, 2008

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

Justyna Brasuń , Marek Cebrat , Aleksandra Sochacka , Olimpia Gładysz and Jolanta Świątek-Kozłowska

Dalton Trans., 2008, 4978-4980

DOI: 10.1039/B807799A
Received 08 May 2008, Accepted 08 Jul 2008
First published on the web 06 Aug 2008

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Abstract
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A new vasopressin analogue, [His^1,6]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, N_Im, N_{Im(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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Justyna Brasuń
Marek Cebrat
Aleksandra Sochacka
Olimpia Gładysz
Jolanta Świątek-Kozłowska

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Dalton Transactions

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

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