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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorGroutas, William C.en_US
dc.contributor.authorBrubaker, Michael J.en_US
dc.contributor.authorStanga, Michael A.en_US
dc.contributor.authorCastrisos, J.C.en_US
dc.contributor.authorCrowley, J.P.en_US
dc.contributor.authorSchatz, E. J.en_US
dc.date.accessioned2012-02-06T17:17:27Z
dc.date.available2012-02-06T17:17:27Z
dc.date.issued1989-07-01en_US
dc.identifier2738894en_US
dc.identifier9716531en_US
dc.identifierR01 HL38048en_US
dc.identifier.citationJournal of medicinal chemistry. 1989 Jul; 32(7): 1607-11.en_US
dc.identifier.issn0022-2623en_US
dc.identifier.urihttp://hdl.handle.net/10057/4424
dc.descriptionFull text of this article is not available in SOAR.en_US
dc.description.abstractA series of compounds derived from 3-alkyl-N-hydroxysuccinimide have been synthesized and their inhibitory activity toward human leukocyte elastase has been investigated. Compounds having an isobutyl or isopropyl group at the C-3 position have been found to be particularly effective inactivators of the enzyme. The introduction of a trans-styryl group (as in compounds 16 and 18) results in a drastic enhancement in inhibitory activity indicative of a favorable interaction between the phenyl ring and the S2' subsite of the enzyme. The compounds were found to be highly stable in buffer solution with no apparent change in structural integrity after 17 h (the period of observation). Studies with model compounds and high-field NMR indicate that these compounds function as mechanism-based inhibitors of the enzyme. Porcine pancreatic elastase is not inhibited by these compounds, while chymotrypsin and human leukocyte cathepsin G are also efficiently inactivated.en_US
dc.description.sponsorshipNHLBI NIH HHSen_US
dc.format.extent1607-11en_US
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesJournal of medicinal chemistryen_US
dc.relation.ispartofseriesJ. Med. Chem.en_US
dc.sourceNLMen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshAnimalsen_US
dc.subject.meshChemical Phenomenaen_US
dc.subject.meshChemistryen_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshHumansen_US
dc.subject.meshKineticsen_US
dc.subject.meshLeukocyte Elastaseen_US
dc.subject.meshPancreas/enzymologyen_US
dc.subject.meshPancreatic Elastase/metabolismen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.subject.meshSuccinimides/analysisen_US
dc.subject.meshSwineen_US
dc.subject.meshSuccinimides/pharmacologyen_US
dc.titleInhibition of human leukocyte elastase by derivatives of N-hydroxysuccinimide. A structure-activity-relationship studyen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1989, American Chemical Societyen_US


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