Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs
Accounts of Chemical Research, ISSN: 0001-4842, Vol: 40, Issue: 4, Page: 267-274
2007
- 190Citations
- 97Captures
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Metrics Details
- Citations190
- Citation Indexes189
- 189
- CrossRef178
- Policy Citations1
- Policy Citation1
- Captures97
- Readers97
- 97
Article Description
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 Bi with proteins and enzymes, such as transferrin and lactoferrin, the histidine-rich protein Hpn, and urease, have been characterized. Sb is a prodrug and is bioreduced or activated to its active form Sb 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. © 2007 American Chemical Society.
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