Open AccessMetal Binding Ability of Small Peptides Containing Cysteine Residues
Author(s) -
Lukács Márton,
Csilla Pálinkás Dóra,
Szunyog Györgyi,
Várnagy Katalin
Publication year - 2021
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.202000304
Subject(s) - chemistry , cysteine , peptide , potentiometric titration , metal ions in aqueous solution , metal , stereochemistry , binding site , molecule , peptide sequence , combinatorial chemistry , biochemistry , ion , organic chemistry , enzyme , gene
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)