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3-(Alkylthio)-N-hydroxysuccinimide derivatives: potent inhibitors of human leukocyte elastase

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dc.contributor Wichita State University. Department of Chemistry en_US
dc.contributor.author Groutas, William C. en_US
dc.contributor.author Venkataraman, Radhika en_US
dc.contributor.author Brubaker, Michael J. en_US
dc.contributor.author Epp, Jeffrey B. en_US
dc.contributor.author Chong, Lee S. en_US
dc.contributor.author Stanga, Michael A. en_US
dc.contributor.author McClenahan, Jerald J. en_US
dc.contributor.author Tagusagawa, F. en_US
dc.date.accessioned 2012-02-06T17:15:24Z
dc.date.available 2012-02-06T17:15:24Z
dc.date.issued 1993-08-07 en_US
dc.identifier 8343527 en_US
dc.identifier 0217513 en_US
dc.identifier HL 38048 en_US
dc.identifier.citation Biochimica et biophysica acta. 1993 Aug 7; 1164(3): 283-8. en_US
dc.identifier.issn 0006-3002 en_US
dc.identifier.uri http://hdl.handle.net/10057/4234
dc.description Full text of this article is not available in SOAR. en_US
dc.description.abstract A series of 3-(alkylthio)-N-hydroxysuccinimide derivatives was synthesized and their inhibitory activity towards human leukocyte elastase (HLE) was investigated. The interaction of the compounds having a 3-alkylthioether side chain (compounds 1 and 2) with HLE was found to involve rapid acylation of the enzyme, followed by total regain of enzymatic activity within 3 h. Interestingly, compounds 3-8, having an oxidized thioether side chain, were found to be highly effective, time-dependent, irreversible inhibitors of the enzyme. The k(obs)/I values for compounds 3-8 ranged between 890 and 24,000 M-1 s-1. These findings demonstrate that, unlike the physiological inhibitor of HLE (alpha-1-proteinase inhibitor), which is inactivated upon oxidation, low-molecular-weight compounds retain and/or show enhanced inhibitory activity towards HLE upon oxidation of the thioether side chain and lay the groundwork for the development of compounds that embody proteinase inhibitory and antioxidant activity. en_US
dc.description.sponsorship NHLBI NIH HHS en_US
dc.format.extent 283-8 en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Biochimica et biophysica acta en_US
dc.relation.ispartofseries Biochim. Biophys. Acta en_US
dc.source NLM en_US
dc.subject Comparative Study en_US
dc.subject Research Support, U.S. Gov't, P.H.S. en_US
dc.subject.mesh Acylation en_US
dc.subject.mesh Enzyme Inhibitors/chemical synthesis en_US
dc.subject.mesh Humans en_US
dc.subject.mesh Leukocytes/enzymology en_US
dc.subject.mesh Models, Molecular en_US
dc.subject.mesh Pancreatic Elastase/antagonists & inhibitors en_US
dc.subject.mesh Structure-Activity Relationship en_US
dc.subject.mesh Succinimides/chemistry en_US
dc.subject.mesh Sulfides/chemical synthesis en_US
dc.subject.mesh alpha 1-Antitrypsin/pharmacology en_US
dc.subject.mesh Succinimides/chemical synthesis en_US
dc.subject.mesh Succinimides/pharmacology en_US
dc.subject.mesh Sulfides/chemistry en_US
dc.title 3-(Alkylthio)-N-hydroxysuccinimide derivatives: potent inhibitors of human leukocyte elastase en_US
dc.type Article en_US
dc.coverage.spacial Netherlands en_US
dc.description.version peer reviewed en_US
dc.rights.holder Copyright © 1993, Elsevie en_US

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