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Updated: Nov 9, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Metal Binding Ability of Small Peptides Containing Cysteine Residues
Márton Lukács1, Dóra Csilla Pálinkás1, Györgyi Szunyog1
1Department of Inorganic and Analytical Chemistry, University of Debrecen, Egyetem tér 1, 4032, Debrecen, Hungary.
Abstract:
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)
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