Issue 28, 2010
From the journal:

Dalton Transactions

The unusual coordination abilities of the peptides with βXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(ii) binding

Justyna Brasuń,*a   Hanna Czapor,a   Agnieszka Matera-Witkiewicz,a   Aleksandra Kotynia,a   Aleksandra Sochackab  and  Marek Cebratb  

* Corresponding authors

a Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, Wrocław, Poland
E-mail: jbrasun@chnorg.am.wroc.pl
Fax: +48-071-784-03-36
Tel: +48-071-784-03-30

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

Abstract

The coordination abilities of tetrapeptides containing β-amino acids towards Cu(II) ions are presented. The studied tetrapeptides were: Ac-βAlaHisGlyHis, βAlaHisGlyHis, Ac-βAspHisGlyHis, βAspHisGlyHis, Ac-βAspHisGly-DHis and βAspHisGly-DHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal–ligand complexes and the role of free -αCOO− side chain group in metal binding. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.

Graphical abstract: The unusual coordination abilities of the peptides with βXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(ii) binding

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Article information

DOI
https://doi.org/10.1039/B923371G
Article type
Paper
Submitted
09 Nov 2009
Accepted
07 May 2010
First published
11 Jun 2010

Dalton Trans., 2010,39, 6518-6523

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The unusual coordination abilities of the peptides with βXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(II) binding

J. Brasuń, H. Czapor, A. Matera-Witkiewicz, A. Kotynia, A. Sochacka and M. Cebrat, Dalton Trans., 2010, 39, 6518 DOI: 10.1039/B923371G

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