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Inne
Polythiol binding to biologically relevant metal ions.
Autorzy
Rok wydania
2011
Czasopismo
Numer woluminu
40
Strony
10434-10439
DOI
10.1039/c1dt10562k
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The coordination properties of three peptides with CXXC motif: Ac-GCASCDNCRACKK-NH2, Ac-GCASCDNCRAAKK-NH2 and Ac-GCASCDNARAAKK-NH2 as donors of four, three and two thiol ligands for Ni2+,Cd2+, Zn2+ and Bi3+ were studied by potentiometric titrations, UV-Vis and CD spectra measurements. Since the stability of the complexes is closely connected with the amount of the metal- bound cysteine sulfurs, competition plots of the complexes of peptides with 2, 3 and 4 cysteines further prove the involvement of all thiols in the metal ion binding. Furthermore, the sulfur- bound zinc complexes appear to be much more stable than the sulfur- bound nickel ones. The stabilities of the studied complexes decreases in the series Bi3+ ≫ Cd2+ > Zn2+ > Ni2+.
Adres publiczny
http://dx.doi.org/ 10.1039/c1dt10562k
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