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dc.identifier.urihttp://hdl.handle.net/11401/77102
dc.description.sponsorshipThis work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.en_US
dc.formatMonograph
dc.format.mediumElectronic Resourceen_US
dc.language.isoen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dc.typeThesis
dcterms.abstractAmyloid formation in vivo plays a role in the pathology of more than 25 diseases. Amyloid formation by Islet Amyloid Polypeptide (IAPP) in the pancreas is a pathophysiological feature of type-2 diabetes. Much work has been performed in order to unravel the mechanisms of IAPP amyloid formation in vitro and recent studies suggest that toxic oligomers are generated during the formation of amyloids. Thus, it may be useful to look for compounds that accelerate fibril formation and reduce the lifetime of toxic intermediates. (S)-(+)-Flurbiprofen has been previously proven to accelerate IAPP amyloid formation. Computational simulation suggested the N-terminus of IAPP plays an important role in the interaction. In order to further understand the mechanism, the effect of (S)-(+)-Flurbiprofen were tested with different mutants of IAPP. The results suggest that the overall charge of IAPP is important in the interaction between negatively charged (S)-(+)-Flurbiprofen and positively charged IAPP. Moreover, a new compound, 4-[(4-chlorophenyl) thio] thiophene-3-carboxylic acid was identified and shown to accelerate amyloid formation by IAPP.
dcterms.available2017-09-20T16:51:58Z
dcterms.contributorRaleigh, Daniel Pen_US
dcterms.contributorLaughlin, Scotten_US
dcterms.contributorGreen, David.en_US
dcterms.creatorChen, Yuan
dcterms.dateAccepted2017-09-20T16:51:58Z
dcterms.dateSubmitted2017-09-20T16:51:58Z
dcterms.descriptionDepartment of Chemistry.en_US
dcterms.extent90 pg.en_US
dcterms.formatMonograph
dcterms.formatApplication/PDFen_US
dcterms.identifierhttp://hdl.handle.net/11401/77102
dcterms.issued2015-08-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2017-09-20T16:51:58Z (GMT). No. of bitstreams: 1 Chen_grad.sunysb_0771M_11824.pdf: 7646882 bytes, checksum: 8bc53bd2e8751d3dc614a8a424a88117 (MD5) Previous issue date: 2014en
dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectChemistry
dcterms.titleAmyloid Accelerators: Small Molecules that Accelerate Amyloid Formation by Amylin
dcterms.typeThesis


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