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Issue 43, 2014
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Specific binding of Zn2+, Cd2+ and Ni2+ ions by a cyclic four-cysteinyl peptide

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Abstract

The metal binding abilities of the GCASCDNCRACKK cyclic peptide towards Zn2+, Cd2+ and Ni2+ ions were studied by potentiometric and spectroscopic methods. The aim of this work was to understand the impact of cyclization on the peptide binding mode and the stability of the formed metal complexes when compared to its linear Ac-GCASCDNCRACKK-NH2 analogue. The obtained results clearly indicate that in the case of Cd2+ and Ni2+ complexes, the cyclization of the coordinating peptide distinctly increases the complex stability in the whole pH range studied. Surprisingly, different results were obtained for Zn2+ complexes. The peptide cyclization seems to prevent the binding of all four available cysteinyl residues to the Zn2+ ion, resulting in the reduced stability of the respective complexes.

Graphical abstract: Specific binding of Zn2+, Cd2+ and Ni2+ ions by a cyclic four-cysteinyl peptide

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Publication details

The article was received on 31 May 2014, accepted on 03 Jul 2014 and first published on 22 Jul 2014


Article type: Paper
DOI: 10.1039/C4DT01614A
Dalton Trans., 2014,43, 16207-16212

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    Specific binding of Zn2+, Cd2+ and Ni2+ ions by a cyclic four-cysteinyl peptide

    K. Krzywoszynska and H. Kozlowski, Dalton Trans., 2014, 43, 16207
    DOI: 10.1039/C4DT01614A

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