Polarographic investigations on the complexation of cadmium and zinc by thiol peptides

Abstract
Complex formation of Cd2+ and Zn2+ with thiol derivatives has been investigated by differential pulse polarography. The binding of Cd2+ and Zn2+ with cysteine (CySH), glutathione (GSH) and the model peptide N‐acetyl‐cysteine‐methylamide (ASH) reveals different stoichiometry. Thus, Cd2+ forms 1:1 and 1:2 complexes with CySH while 1:2 and 1:4 complexes have been observed with GSH and ASH, respectively. Overall formation constants of Cd2+ with CySH (Iogβ 2 15.3) and with GSH (Iogβ52 14.4) have been estimated using competitive complexation with nitrilotriacetic acid (NTA). Investigation of competition between Zn2+ and Cd2+ for the thiol complexation has underlined the role played by the amino group in CySH for the stabilization of Zn complexes in contrary to Cd complexes.

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