Inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamides

dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorLi, Yien_US
dc.contributor.authorYang, Qingliangen_US
dc.contributor.authorDou, Dengfengen_US
dc.contributor.authorAlliston, Kevin R.en_US
dc.contributor.authorGroutas, William C.en_US
dc.coverage.spacialEnglanden_US
dc.date.accessioned2012-02-06T17:17:02Z
dc.date.available2012-02-06T17:17:02Z
dc.date.issued2008-01-15en_US
dc.descriptionClick on the DOI link below to access the article.en_US
dc.description.abstractThe interaction of a series of 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamides with neutrophil-derived serine proteases was investigated. The nature of the amino acid component, believed to be oriented toward the S' subsites, had a profound effect on enzyme selectivity. This series of compounds were found to be potent, time-dependent inhibitors of human neutrophil elastase (HNE) and were devoid of any inhibitory activity toward neutrophil proteinase 3 (PR 3) and cathepsin G (Cat G). The results of these studies demonstrate that exploitation of differences in the S' subsites of HNE and PR 3 can lead to highly selective inhibitors of HNE.en_US
dc.description.sponsorshipNHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHSen_US
dc.description.versionpeer revieweden_US
dc.format.extent692-8en_US
dc.identifier17976994en_US
dc.identifier9413298en_US
dc.identifierS0968-0896(07)00909-1en_US
dc.identifierHL 57788/ R01 HL057788-02/ R01 HL057788-03/ R01 HL057788-04/ R01 HL057788-05/ R01 HL057788-06/ R01 HL057788-07/ R01 HL057788-08en_US
dc.identifier.citationBioorganic & medicinal chemistry. 2008 Jan 15; 16(2): 692-8.en_US
dc.identifier.issn1464-3391en_US
dc.identifier.issn0968-0896en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.bmc.2007.10.041en_US
dc.identifier.urihttp://hdl.handle.net/10057/4384
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.ispartofseriesBioorganic & medicinal chemistryen_US
dc.relation.ispartofseriesBioorg. Med. Chem.en_US
dc.rights.holderCopyright © 2008, Elsevieren_US
dc.sourceNLMen_US
dc.subjectResearch Support, N.I.H., Extramuralen_US
dc.subject.meshAlgorithmsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCathepsin Gen_US
dc.subject.meshCathepsins/antagonists & inhibitorsen_US
dc.subject.meshCombinatorial Chemistry Techniquesen_US
dc.subject.meshDrug Designen_US
dc.subject.meshHumansen_US
dc.subject.meshLeukocyte Elastase/antagonists & inhibitorsen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshMyeloblastin/antagonists & inhibitorsen_US
dc.subject.meshSerine Endopeptidasesen_US
dc.subject.meshSerine Proteinase Inhibitors/chemical synthesisen_US
dc.subject.meshSulfonamides/chemical synthesisen_US
dc.subject.meshThiadiazoles/chemical synthesisen_US
dc.subject.meshSerine Proteinase Inhibitors/chemistryen_US
dc.subject.meshSerine Proteinase Inhibitors/pharmacologyen_US
dc.subject.meshSulfonamides/chemistryen_US
dc.subject.meshSulfonamides/pharmacologyen_US
dc.subject.meshThiadiazoles/chemistryen_US
dc.subject.meshThiadiazoles/pharmacologyen_US
dc.titleInactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1 dioxide-based sulfonamidesen_US
dc.typeArticleen_US
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