Bioinorganic chemistry of bismuth and antimony: target sites of metallodrugs.

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Ge R, Sun H

Bioinorganic chemistry of bismuth and antimony: target sites of metallodrugs.

Acc Chem Res. 2007 Apr;40(4):267-74. Epub 2007 Mar 2.

PubMed ID
17330963 [ View in PubMed
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Abstract

The biocoordination chemistry of antimony and bismuth has been extensively investigated due to the historical use of these metals in medicine. Structures of bismuth antiulcer agents and interactions of Bi3+ with proteins and enzymes, such as transferrin and lactoferrin, the histidine-rich protein Hpn, and urease, have been characterized. Sb5+ is a prodrug and is bioreduced or activated to its active form Sb3+ intracellularly. Antimony binds to biomolecules, such as glutathione, trypanothione, and nucleotides, and forms binary and ternary complexes, which may allow it to be trafficked in cells. These studies have improved our understanding of the mechanism of action of bismuth and antimony drugs, which in turn allows the future design of drugs.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
Bismuth subsalicylateSerotransferrinProteinHumans
Unknown
Not AvailableDetails