Metal Binding Ability of Small Peptides Containing Cysteine Residues |
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Authors: | Márton Lukács Dóra Csilla Pálinkás Dr. Györgyi Szunyog Prof. Katalin Várnagy |
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Affiliation: | Department of Inorganic and Analytical Chemistry, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary |
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Abstract: | The Cd(II)-, Pb(II)-, Ni(II)- and Zn(II)-complexes of small terminally protected peptides containing CXXX, XXXC, XCCX, CXnC (n=1–3) sequences have been studied with potentiometric, UV/Vis and CD spectroscopic techniques. The cysteine thiolate group is the primary binding site for all studied metal ions, but the presence of a histidyl or aspartyl side chain in the molecule contributes to the stability of the complexes. For two-cysteine containing peptides the (S−,S−) coordinated species are formed in the physiological pH range and the stability increases in the Ni(II)
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Keywords: | cysteine containing peptides metal complexes stability constant spectroscopic measurements selectivity |
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