Metal Binding Ability of Small Peptides Containing Cysteine Residues.

The Cd(II)-, Pb(II)-, Ni(II)- and Zn(II)-complexes of small terminally protected peptides containing CXXX, XXXC, XCCX, CXn C (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)

Keywords:

• Metal ions in aqueous solution
• Stereochemistry
• Molecule
• Chemistry
• Peptide
• Binding site
• Stability constants of complexes
• Side chain
• Cysteine
• Potentiometric titration

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