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dc.contributor.advisorBlagg, Brian S. J.
dc.contributor.authorLubbers, Donna Jeanne
dc.date.accessioned2009-02-02T05:56:34Z
dc.date.available2009-02-02T05:56:34Z
dc.date.issued2008-01-01
dc.date.submitted2008
dc.identifier.otherhttp://dissertations.umi.com/ku:10012
dc.identifier.urihttp://hdl.handle.net/1808/4338
dc.description.abstractAs C−terminal inhibitors of a 90−kDa heat shock protein (Hsp90), novobiocin and its derivatives are a significant part of an emerging class of cancer chemotherapeutic agents. Previous studies have shown that analogues of the coumarin and benzamide moieties of novobiocin exhibit more than a 1000−fold improvement in activity over the parent compound. This thesis describes synthetic efforts toward the completion of noviose mimics to determine moieties that are critical for binding or can be altered for improved activity. Additionally, in the absence of a co−crystal structure for the Hsp90 C−terminus, there is a need to develop an accurate model to assist in efficient drug design. This work describes the use of molecular modeling and docking software to design new, potentially useful models of C−terminal interactions.
dc.format.extent101 pages
dc.language.isoEN
dc.publisherUniversity of Kansas
dc.rightsThis item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
dc.subjectOrganic chemistry
dc.subjectPharmaceutical chemistry
dc.subjectChemistry
dc.subjectC-terminus
dc.subjectComputational
dc.subjectHsp90
dc.subjectNovobiocin
dc.subjectSynthesis
dc.titleSynthetic and computational efforts toward the understanding and development of novobiocin-derived inhibitors of Hsp90
dc.typeThesis
dc.contributor.cmtememberTimmermann, Barbara N.
dc.contributor.cmtememberHanson, Paul R.
dc.thesis.degreeDisciplineMedicinal Chemistry
dc.thesis.degreeLevelM.S.
kusw.oastatusna
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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