Issue 37, 2008
From the journal:

Dalton Transactions

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

Justyna Brasuń,*a   Marek Cebrat,b   Aleksandra Sochacka,b   Olimpia Gładysza  and  Jolanta Świątek-Kozłowskaa  

* Corresponding authors

a Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, Wrocław, Poland
E-mail: jbrasun@chnorg.am.wroc.pl
Fax: +48-71-7840336
Tel: +48-71-7840330

b Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, Wrocław, Poland

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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Article information

DOI
https://doi.org/10.1039/B807799A
Article type
Communication
Submitted
08 May 2008
Accepted
08 Jul 2008
First published
06 Aug 2008

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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