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- PMID: 17330963
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Article: Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs
Title | Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs |
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Authors | |
Issue Date | 2007 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/achre4/about.html |
Citation | Accounts Of Chemical Research, 2007, v. 40 n. 4, p. 267-274 How to Cite? |
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. © 2007 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/168109 |
ISSN | 2023 Impact Factor: 16.4 2023 SCImago Journal Rankings: 5.948 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ge, R | en_US |
dc.contributor.author | Sun, H | en_US |
dc.date.accessioned | 2012-10-08T03:15:11Z | - |
dc.date.available | 2012-10-08T03:15:11Z | - |
dc.date.issued | 2007 | en_US |
dc.identifier.citation | Accounts Of Chemical Research, 2007, v. 40 n. 4, p. 267-274 | en_US |
dc.identifier.issn | 0001-4842 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/168109 | - |
dc.description.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. © 2007 American Chemical Society. | en_US |
dc.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/achre4/about.html | en_US |
dc.relation.ispartof | Accounts of Chemical Research | en_US |
dc.subject.mesh | Antimony - Chemistry - Metabolism | en_US |
dc.subject.mesh | Bismuth - Chemistry - Metabolism | en_US |
dc.subject.mesh | Cations | en_US |
dc.subject.mesh | Drug Design | en_US |
dc.subject.mesh | Enzymes - Chemistry - Metabolism | en_US |
dc.subject.mesh | Glutathione - Analogs & Derivatives - Chemistry - Metabolism | en_US |
dc.subject.mesh | Lactoferrin - Chemistry - Metabolism | en_US |
dc.subject.mesh | Magnetic Resonance Spectroscopy | en_US |
dc.subject.mesh | Molecular Structure | en_US |
dc.subject.mesh | Nucleotides - Chemistry - Metabolism | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Proteins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Spectrometry, Mass, Electrospray Ionization | en_US |
dc.subject.mesh | Spermidine - Analogs & Derivatives - Chemistry - Metabolism | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.subject.mesh | Transferrin - Chemistry - Metabolism | en_US |
dc.subject.mesh | Urease - Chemistry - Metabolism | en_US |
dc.title | Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sun, H:hsun@hkucc.hku.hk | en_US |
dc.identifier.authority | Sun, H=rp00777 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1021/ar600001b | en_US |
dc.identifier.pmid | 17330963 | - |
dc.identifier.scopus | eid_2-s2.0-34248380121 | en_US |
dc.identifier.hkuros | 132938 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-34248380121&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 40 | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.spage | 267 | en_US |
dc.identifier.epage | 274 | en_US |
dc.identifier.isi | WOS:000245735400005 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Ge, R=7005525090 | en_US |
dc.identifier.scopusauthorid | Sun, H=7404827446 | en_US |
dc.identifier.citeulike | 3813167 | - |
dc.identifier.issnl | 0001-4842 | - |