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-NH(2)) and to a reference peptide (Ac-CHCH-NH(2)). 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antacids / pharmacology
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Antacids / therapeutic use
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Anti-Ulcer Agents / chemistry
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Anti-Ulcer Agents / pharmacology*
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Bacterial Proteins / chemistry
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Bacterial Proteins / drug effects*
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Binding Sites
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Bismuth / chemistry*
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Bismuth / metabolism
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Bismuth / pharmacology
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Circular Dichroism
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / drug effects*
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Helicobacter Infections / drug therapy
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Helicobacter Infections / microbiology
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Helicobacter pylori / chemistry*
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Helicobacter pylori / metabolism
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Histidine / chemistry
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Histidine / metabolism
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Humans
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Nickel / chemistry*
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Nickel / metabolism
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Nickel / pharmacology
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Nuclear Magnetic Resonance, Biomolecular
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Potentiometry
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Protein Structure, Tertiary
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Spectrophotometry, Ultraviolet
Substances
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Antacids
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Anti-Ulcer Agents
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Bacterial Proteins
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Heat-Shock Proteins
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HspA protein, bacteria
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Oligopeptides
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Histidine
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Nickel
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Bismuth