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Metal Binding Ability of Small Peptides Containing Cysteine Residues
- Source :
- ChemistryOpen, ChemistryOpen, Vol 10, Iss 4, Pp 451-463 (2021)
- Publication Year :
- 2021
- Publisher :
- John Wiley and Sons Inc., 2021.
-
Abstract
- The Cd(II)‐, Pb(II)‐, Ni(II)‐ and Zn(II)‐complexes of small terminally protected peptides containing CXXX, XXXC, XCCX, CXnC (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)<br />The systematic study of small cysteine containing peptides reveals the outstanding Pb(II)‐ and Cd(II)‐binding ability of peptides with CXnC (n=0–3) sequence. This is well demonstrated by pM values calculated for different metal‐peptide systems at pH 7 (cL=0.010 mM, cM=0.001 mM).
Details
- Language :
- English
- ISSN :
- 21911363
- Volume :
- 10
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- ChemistryOpen
- Accession number :
- edsair.pmid.dedup....c8671cad8db6a96a257d02cdec467cd4