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Article: Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs

TitleBioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs
Authors
Issue Date2007
PublisherAmerican 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?
AbstractThe 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 Identifierhttp://hdl.handle.net/10722/168109
ISSN
2015 Impact Factor: 22.003
2015 SCImago Journal Rankings: 11.465
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGe, Ren_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2012-10-08T03:15:11Z-
dc.date.available2012-10-08T03:15:11Z-
dc.date.issued2007en_US
dc.identifier.citationAccounts Of Chemical Research, 2007, v. 40 n. 4, p. 267-274en_US
dc.identifier.issn0001-4842en_US
dc.identifier.urihttp://hdl.handle.net/10722/168109-
dc.description.abstractThe 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.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/achre4/about.htmlen_US
dc.relation.ispartofAccounts of Chemical Researchen_US
dc.subject.meshAntimony - Chemistry - Metabolismen_US
dc.subject.meshBismuth - Chemistry - Metabolismen_US
dc.subject.meshCationsen_US
dc.subject.meshDrug Designen_US
dc.subject.meshEnzymes - Chemistry - Metabolismen_US
dc.subject.meshGlutathione - Analogs & Derivatives - Chemistry - Metabolismen_US
dc.subject.meshLactoferrin - Chemistry - Metabolismen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshNucleotides - Chemistry - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProteins - Chemistry - Metabolismen_US
dc.subject.meshSpectrometry, Mass, Electrospray Ionizationen_US
dc.subject.meshSpermidine - Analogs & Derivatives - Chemistry - Metabolismen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshTransferrin - Chemistry - Metabolismen_US
dc.subject.meshUrease - Chemistry - Metabolismen_US
dc.titleBioinorganic chemistry of bismuth and antimony: Target sites of metallodrugsen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ar600001ben_US
dc.identifier.pmid17330963-
dc.identifier.scopuseid_2-s2.0-34248380121en_US
dc.identifier.hkuros132938-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34248380121&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume40en_US
dc.identifier.issue4en_US
dc.identifier.spage267en_US
dc.identifier.epage274en_US
dc.identifier.isiWOS:000245735400005-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridGe, R=7005525090en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.citeulike3813167-

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