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dc.contributor.advisorGroutas, William C.en_US
dc.contributor.authorYang, Qingliang
dc.date.accessioned2007-02-08T01:43:53Z
dc.date.available2007-02-08T01:43:53Z
dc.date.issued2006-12
dc.identifier.othert06112
dc.identifier.urihttp://hdl.handle.net/10057/444
dc.descriptionThesis (M.S.)--Wichita State University, College of Liberal Arts and Sciences, Dept. of Chemistry.en
dc.description"December 2006."en
dc.descriptionIncludes bibliographical references (leaves 34-37)en
dc.description.abstractThe neutrophil-derived serine proteases human leukocyte elastase (HLE) and proteinase 3 (PR3) have been implicated in various inflammatory diseases such as pulmonary emphysema, chronic bronchitis, asthma, cystic fibrosis, rheumatoid arthritis, psoriasis, and others. Poor regulation of the activity of these enzymes by their endogenous protein inhibitors is believed to result in the degradation of the major components of intracellular matrix. Agents that function as potent and selective inhibitors of these enzymes are of potential therapeutic value. The research described herein was an attempt to design and synthesize a class of non-covalent inhibitors of HLE and PR3 based on the cyclosulfamide scaffold. However during the course of these studies a new class of covalent inhibitors of HLE was discovered.en
dc.format.extentviii, 37 leaves: ill., digital, PDF file.
dc.format.extent259235 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.rightsCopyright Qingliang Yang, 2006. All rights reserved.en
dc.subject.lcshElectronic dissertationsen
dc.titleA new class of carbamoylating agents based on the cyclosulfamide scaffolden
dc.typeThesisen


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