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The C terminus of HspA–a potential target for native Ni(II) and Bi(III) anti-ulcer drugs.
Autorzy
Rok wydania
2010
Czasopismo
Numer woluminu
39
Strony
5814-5826
DOI
10.1039/C0DT00013B
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
HspA, a protein crucial for nickel homeostasis in Helicobacter pylori (H. pylori), has a unique histidine- and cysteine-rich domain at the C terminus. In this work, we compared the coordination of nickel (the natural co-factor) and bismuth (inhibitor) to this domain (Ac-ACCHDHKKH-NH2) and to a reference peptide (Ac-CHCH-NH2). Potentiometric, CD, UV-Vis spectroscopic and NMR methods have shown that bismuth binds incomparably stronger than nickel; the same data shows the impact of histidines on such a binding. Our results are in good agreement with earlier biological data and suggest that HspA can be a potential target of the bismuth anti-ulcer drug against H. pylori.
Adres publiczny
http://dx.doi.org/ 10.1039/C0DT00013B