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.

ROWINSKA ZYREK, M., Witkowska, D., Valensin, D., Kamysz, W., & Kozlowski, H. (2010). The C terminus of HspA - A potential target for native Ni(II) and Bi(III) anti-ulcer drugs. DALTON TRANSACTIONS, 39, 5814-5826 [10.1039/c0dt00013b].

The C terminus of HspA - A potential target for native Ni(II) and Bi(III) anti-ulcer drugs

VALENSIN, DANIELA;
2010

Abstract

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.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/24239
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