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dc.contributor.authorGillis, Margaret A.L.
dc.date.accessioned2014-07-24T16:43:52Z
dc.date.available2014-07-24T16:43:52Z
dc.date.issued2014-07-24
dc.identifier.urihttp://hdl.handle.net/10222/53125
dc.description.abstractThe most common form of neurodegenerative dementia is Alzheimer’s disease. One of the hallmarks of the disease is the presence of plaques, which is an aggregation of a peptide called amyloid-β. This aggregation occurs because of misfolding of the protein. Recent studies have shown that polyphenols within different types of foods may have potential to have an anti-aggregate effect on amyloid-β. This study focused on using molecular modeling to dock various polyphenols to two regions on the amyloid β-peptide: H13HQK and L17VFF. These areas are often targeted by anti-aggregate drugs for Alzheimer’s. The polyphenols that were studied were (+)-catechin, (-)-epicatechin, cyanidin, and quebecol. An analysis of binding energies and interactions obtained using the CHARMM22 force field showed that these molecules have some affinity to HHQK but more so toward LVFF. Cyanidin, however, showed very little affinity to HHQK.en_US
dc.language.isoen_USen_US
dc.subjectApplesen_US
dc.subjectbeta-amyloiden_US
dc.subjectcomputational chemistryen_US
dc.subjectAlzheimer's Diseaseen_US
dc.subjectPolyphenolsen_US
dc.titleA Molecular Mechanics Study of Natural Product Polyphenols Interacting with beta-Amyloiden_US
dc.date.defence2014-07-04
dc.contributor.departmentDepartment of Chemistryen_US
dc.contributor.degreeMaster of Scienceen_US
dc.contributor.external-examinerN/Aen_US
dc.contributor.graduate-coordinatorDr. Mark Stradiottoen_US
dc.contributor.thesis-readerDr. Russell Boyden_US
dc.contributor.thesis-readerDr. Axel Beckeen_US
dc.contributor.thesis-supervisorDr. Donald Weaver and Dr. Mark Stradiottoen_US
dc.contributor.ethics-approvalNot Applicableen_US
dc.contributor.manuscriptsNot Applicableen_US
dc.contributor.copyright-releaseNot Applicableen_US
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