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Article: Interaction of antimony tartrate with the tripeptide glutathione implication for its mode of action

TitleInteraction of antimony tartrate with the tripeptide glutathione implication for its mode of action
Authors
KeywordsAntimony
Glutathione
Nuclear magnetic resonance
Red blood cells
Issue Date2000
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 2000, v. 267 n. 17, p. 5450-5457 How to Cite?
AbstractThe tripeptide glutathione (γ-L-Glu-L-Cys-Gly, GSH) is thought to play an important role in the biological processing of antimony drugs. We have studied the complexation of the antileishmanial drug potassium antimony(III) tartrate to GSH in both aqueous solution and intact red blood cells by NMR spectroscopy and electrospray ionization mass spectrometry. The deprotonated thiol group of the cysteine residue is shown to be the only binding site for Sb(III), and a complex with the stoichiometry [Sb(GS)3] is formed. The stability constant for [Sb(GS)3] was determined to be log K 25 (I = 0.1 M, 298 K) based on a competition reaction between tartrate and GSH at different pH* values. In spite of being highly thermodynamically stable, the complex is kinetically labile. The rate of exchange of GSH between its free and Sb-bound form is pH-dependent, ranging from slow exchange on the 1H-NMR timescale at low pH (2 s-1 at pH 3.2) to relatively rapid exchange at biological pH (> 440 s-1). Such facile exchange may be important in the transport of Sb(III) in various biofluids and tissues in vivo. Our spin-echo 1H-NMR data show that Sb(III) rapidly entered red blood cell walls and was complexed by intracellular glutathione.
Persistent Identifierhttp://hdl.handle.net/10722/69617
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Hen_HK
dc.contributor.authorYan, SCen_HK
dc.contributor.authorCheng, WSen_HK
dc.date.accessioned2010-09-06T06:15:18Z-
dc.date.available2010-09-06T06:15:18Z-
dc.date.issued2000en_HK
dc.identifier.citationEuropean Journal Of Biochemistry, 2000, v. 267 n. 17, p. 5450-5457en_HK
dc.identifier.issn0014-2956en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69617-
dc.description.abstractThe tripeptide glutathione (γ-L-Glu-L-Cys-Gly, GSH) is thought to play an important role in the biological processing of antimony drugs. We have studied the complexation of the antileishmanial drug potassium antimony(III) tartrate to GSH in both aqueous solution and intact red blood cells by NMR spectroscopy and electrospray ionization mass spectrometry. The deprotonated thiol group of the cysteine residue is shown to be the only binding site for Sb(III), and a complex with the stoichiometry [Sb(GS)3] is formed. The stability constant for [Sb(GS)3] was determined to be log K 25 (I = 0.1 M, 298 K) based on a competition reaction between tartrate and GSH at different pH* values. In spite of being highly thermodynamically stable, the complex is kinetically labile. The rate of exchange of GSH between its free and Sb-bound form is pH-dependent, ranging from slow exchange on the 1H-NMR timescale at low pH (2 s-1 at pH 3.2) to relatively rapid exchange at biological pH (> 440 s-1). Such facile exchange may be important in the transport of Sb(III) in various biofluids and tissues in vivo. Our spin-echo 1H-NMR data show that Sb(III) rapidly entered red blood cell walls and was complexed by intracellular glutathione.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_HK
dc.relation.ispartofEuropean Journal of Biochemistryen_HK
dc.rightsEuropean Journal of Biochemistry. Copyright © Blackwell Publishing Ltd.en_HK
dc.subjectAntimonyen_HK
dc.subjectGlutathioneen_HK
dc.subjectNuclear magnetic resonanceen_HK
dc.subjectRed blood cellsen_HK
dc.titleInteraction of antimony tartrate with the tripeptide glutathione implication for its mode of actionen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-2956&volume=267&spage=5450&epage=5457&date=2000&atitle=Interaction+of+antimony+tartrate+with+the+tripeptide+glutathione+-+implication+for+its+mode+of+actionen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1046/j.1432-1327.2000.01605.xen_HK
dc.identifier.pmid10951203en_HK
dc.identifier.scopuseid_2-s2.0-0033858554en_HK
dc.identifier.hkuros58746en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033858554&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume267en_HK
dc.identifier.issue17en_HK
dc.identifier.spage5450en_HK
dc.identifier.epage5457en_HK
dc.identifier.isiWOS:000089101400023-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridYan, SC=7401744858en_HK
dc.identifier.scopusauthoridCheng, WS=18436247800en_HK

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