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Metal Binding Ability of Small Peptides Containing Cysteine Residues.

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

SUBMITTER: Lukacs M

PROVIDER: S-EPMC8028610 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Metal Binding Ability of Small Peptides Containing Cysteine Residues.

Lukács Márton M Csilla Pálinkás Dóra D Szunyog Györgyi G Várnagy Katalin K

ChemistryOpen 20210401 4

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-</ ...[more]

PMID: 33830669

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