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Article: Comparative analysis of binding affinities between styrene and mammalian CYP2E1 by bioinformatics approaches

TitleComparative analysis of binding affinities between styrene and mammalian CYP2E1 by bioinformatics approaches
Authors
Issue Date2011
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0963-9292
Citation
Ecotoxicology, 2011, v. 20 n. 5, p. 1041-1046 How to Cite?
AbstractAbstract:: Cytochrome P450 2E1 (CYP2E1) is a cytochrome P450 enzyme involved in styrene metabolism. This study compared the binding affinities between styrene and 11 mammalian CYP2E1 systems using bioinformatics methods. Firstly, amino acid sequences of CYP2E1s were obtained from the Swiss-Prot database. Then, taking the crystal structure of human CYP2E1 as a template, 3D models of the CYP2E1s of other mammals were constructed using the SWISS-MODEL program. Finally, the generated homology models were applied to calculate their docking capacities against styrene and polystyrene using the Surflex-Dock program, which could automatically dock ligands into a receptor's ligand binding site using a protomol based approach and assess the affinity by an empirically derived scoring function. Docking experiments showed that the studied mammalian CYP2E1s had high binding affinities with styrene. For polystyrene, the dimmer of styrene has high binding affinities with CYP2E1s, however, trimer and other high polymers were found hard to be docked into the CYP2E1s. The results of this study indicated that bioinformatics approaches might be useful tools to predict styrene and polystyrene affinities with mammalian CYP2E1s. © 2011 Springer Science+Business Media, LLC.
Persistent Identifierhttp://hdl.handle.net/10722/179241
ISSN
2015 Impact Factor: 2.329
2015 SCImago Journal Rankings: 1.108
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWu, Ben_US
dc.contributor.authorSun, Jen_US
dc.contributor.authorCheng, SPen_US
dc.contributor.authorGu, JDen_US
dc.contributor.authorLi, AMen_US
dc.contributor.authorZhang, XXen_US
dc.date.accessioned2012-12-19T09:53:20Z-
dc.date.available2012-12-19T09:53:20Z-
dc.date.issued2011en_US
dc.identifier.citationEcotoxicology, 2011, v. 20 n. 5, p. 1041-1046en_US
dc.identifier.issn0963-9292en_US
dc.identifier.urihttp://hdl.handle.net/10722/179241-
dc.description.abstractAbstract:: Cytochrome P450 2E1 (CYP2E1) is a cytochrome P450 enzyme involved in styrene metabolism. This study compared the binding affinities between styrene and 11 mammalian CYP2E1 systems using bioinformatics methods. Firstly, amino acid sequences of CYP2E1s were obtained from the Swiss-Prot database. Then, taking the crystal structure of human CYP2E1 as a template, 3D models of the CYP2E1s of other mammals were constructed using the SWISS-MODEL program. Finally, the generated homology models were applied to calculate their docking capacities against styrene and polystyrene using the Surflex-Dock program, which could automatically dock ligands into a receptor's ligand binding site using a protomol based approach and assess the affinity by an empirically derived scoring function. Docking experiments showed that the studied mammalian CYP2E1s had high binding affinities with styrene. For polystyrene, the dimmer of styrene has high binding affinities with CYP2E1s, however, trimer and other high polymers were found hard to be docked into the CYP2E1s. The results of this study indicated that bioinformatics approaches might be useful tools to predict styrene and polystyrene affinities with mammalian CYP2E1s. © 2011 Springer Science+Business Media, LLC.en_US
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0963-9292en_US
dc.relation.ispartofEcotoxicologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshComputational Biologyen_US
dc.subject.meshCytochrome P-450 Cyp2e1 - Chemistryen_US
dc.subject.meshEnvironmental Pollutants - Chemistryen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshModels, Chemicalen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshStyrene - Chemistryen_US
dc.titleComparative analysis of binding affinities between styrene and mammalian CYP2E1 by bioinformatics approachesen_US
dc.typeArticleen_US
dc.identifier.emailGu, JD: jdgu@hkucc.hku.hken_US
dc.identifier.authorityGu, JD=rp00701en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s10646-011-0643-zen_US
dc.identifier.pmid21424721-
dc.identifier.scopuseid_2-s2.0-79960333804en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79960333804&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume20en_US
dc.identifier.issue5en_US
dc.identifier.spage1041en_US
dc.identifier.epage1046en_US
dc.identifier.isiWOS:000291887500014-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWu, B=55120553300en_US
dc.identifier.scopusauthoridSun, J=35148505000en_US
dc.identifier.scopusauthoridCheng, SP=18039405400en_US
dc.identifier.scopusauthoridGu, JD=7403129601en_US
dc.identifier.scopusauthoridLi, AM=24577638500en_US
dc.identifier.scopusauthoridZhang, XX=35316674200en_US
dc.identifier.citeulike9074162-

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