Show simple item record

dc.contributor.advisorRaleigh, Daniel P.en_US
dc.contributor.authorNoor, Harrisen_US
dc.contributor.otherDepartment of Chemistryen_US
dc.date.accessioned2013-05-22T17:35:19Z
dc.date.available2013-05-22T17:35:19Z
dc.date.issued1-Aug-12en_US
dc.date.submitted12-Augen_US
dc.identifierNoor_grad.sunysb_0771M_11028en_US
dc.identifier.urihttp://hdl.handle.net/1951/59809
dc.description93 pg.en_US
dc.description.abstractAmyloid formation is involved in many human diseases. Examples include Alzheimer's, Huntington's, and Parkinson's disease, and type-2 diabetes. Islet Amyloid Polypeptide (IAPP) is a protein that is co-secreted with insulin in pancreatic beta-cells; however, IAPP is an extremely amyloidogenic protein. There is a considerable amount of interest to develop inhibitors for amyloid formation. A large body of work has been focused on the development of inhibitors for the A-beta peptide of Alzheimer's disease, but fewer inhibitors have been developed for IAPP. In this thesis, small molecules were developed to alter fiber formation kinetics. This thesis described studies of the ability of Morin Hydrate to inhibit and S-Flurbiprofen to accelerate IAPP amyloid formation. Both of these compounds have been analyzed and proposed to be inhibitors of A, but they have not been tested on IAPP. Morin hydrate, a hydroxyflavone, can be found in fruits of plants and S-flurbiprofen is a non-steroidal anti-inflammatory drug (NSAID) that is a derivative of naturally occurring molecules found in plants. It is thought that the toxic intermediates that these amyloidgenic peptides form are the central cause of these amyloidgenic diseases; not necessarily the fibers. These studies demonstrate two different approaches to inhibit amyloid toxicity. One method is to inhibit amyloid formation directly and avoid producing the toxic intermediates. The other method is to accelerate the kinetics at assembly past the toxic oligomeric state straight into fibers. These studies may give a better understanding of the mechanism of amyloid formation and possibly assist in developing effective therapeutic strategies for different amyloidgenic diseases.en_US
dc.description.sponsorshipStony Brook University Libraries. SBU Graduate School in Department of Chemistry. Charles Taber (Dean of Graduate School).en_US
dc.formatElectronic Resourceen_US
dc.language.isoen_USen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.en_US
dc.subject.lcshChemistryen_US
dc.subject.otherAmyloid, IAPP, Inhibitoren_US
dc.titleSmall Molecule Modulators of Amyloid Formation by Islet Amyloid Polypeptideen_US
dc.typeThesisen_US
dc.description.advisorAdvisor(s): Raleigh, Daniel P.. Committee Member(s): Boon, Elizabeth ; Seeliger, Jessica.en_US
dc.mimetypeApplication/PDFen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record