{"@context":"http://iiif.io/api/presentation/2/context.json","@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/manifest.json","@type":"sc:Manifest","label":"Identification and Characterization of an Insulin Based Inhibitor of Amylin and A\u03b240 Amyloid Formation","metadata":[{"label":"dc.description.sponsorship","value":"This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree."},{"label":"dc.format","value":"Monograph"},{"label":"dc.format.medium","value":"Electronic Resource"},{"label":"dc.identifier.uri","value":"http://hdl.handle.net/1951/55365"},{"label":"dc.language.iso","value":"en_US"},{"label":"dc.publisher","value":"The Graduate School, Stony Brook University: Stony Brook, NY."},{"label":"dcterms.abstract","value":"The formation of amyloid fibrils plays a role in a wide range of diseases collectively known as amyloidosis. Amyloid fibrils are formed when peptides or proteins misfold and deposit in tissues and organs. These deposits are a characteristic feature of a number of diseases including Type II diabetes, Alzheimer's disease, and Parkinson's disease. Our lab studies the amyloidogenic peptides Islet Amyloid Polypeptide (IAPP) from type II diabetes and the A\u03b240 and A\u03b242 peptides from Alzheimer's disease. There is intriguing, albeit indirect, evidence that suggests that inhibitors of IAPP amyloid formation may also inhibit amyloid formation by A\u03b2. If true, this suggests a new strategy for designing inhibitors; specifically inhibitors of amyloid formation by one peptide can be used against the other.Insulin is known to be an inhibitor of IAPP. It is made up of an A and B chain and the B chain displays potent inhibitory effects. In addition, a short segment located in the B chain has been showed to bind IAPP and thus might inhibit amyloid formation.Based on these findings, experiments were conducted to test the possible inhibitory effects of insulin, the insulin B chain, and a short fragment from the insulin B chain on A\u03b240 and IAPP.Solid phase peptide synthesis was used to synthesize thee A\u03b240 peptide and a 12-residue fragment of the insulin B chain (IBSF). A new protocol was developed and employed to obtain the kinetic curve of A\u03b240 amyloid formation using Thioflavin-Tbinding fluorescence assays. A\u03b240 was incubated with insulin, the insulin B chain, and IBSF. Transmission electron microscopy was used to observe what had occurred during the incubation and confirm the results of the fluorescence assays. Similar experiments with IAPP were done as well, however, the rate of fibrillization was found to be much slower. This suggested that there is indeed an interaction between these two peptides. Thus, concentration dependent studies and further experimentation were done to better observe and assess these interactions."},{"label":"dcterms.available","value":"2015-04-24T14:45:51Z"},{"label":"dcterms.contributor","value":"Raleigh, Daniel P."},{"label":"dcterms.creator","value":"Barua, Trisha"},{"label":"dcterms.dateAccepted","value":"2012-05-15T18:02:12Z"},{"label":"dcterms.dateSubmitted","value":"2012-05-15T18:02:12Z"},{"label":"dcterms.description","value":"Department of Chemistry"},{"label":"dcterms.format","value":"Monograph"},{"label":"dcterms.identifier","value":"http://hdl.handle.net/11401/71076"},{"label":"dcterms.issued","value":"2010-08-01"},{"label":"dcterms.language","value":"en_US"},{"label":"dcterms.provenance","value":"Made available in DSpace on 2012-05-15T18:02:12Z (GMT). No. of bitstreams: 1\nBarua_grad.sunysb_0771M_10231.pdf: 4644692 bytes, checksum: e4d67b360f18d25d9769ee1b8a73646a (MD5)\n  Previous issue date:    1"},{"label":"dcterms.publisher","value":"The Graduate School, Stony Brook University: Stony Brook, NY."},{"label":"dcterms.subject","value":"Chemistry, Biochemistry --  Biophysics, General"},{"label":"dcterms.title","value":"Identification and Characterization of an Insulin Based Inhibitor of Amylin and A\u03b240 Amyloid Formation"},{"label":"dcterms.type","value":"Thesis"},{"label":"dc.type","value":"Thesis"}],"description":"This manifest was generated dynamically","viewingDirection":"left-to-right","sequences":[{"@type":"sc:Sequence","canvases":[{"@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/canvas/page-1.json","@type":"sc:Canvas","label":"Page 1","height":1650,"width":1275,"images":[{"@type":"oa:Annotation","motivation":"sc:painting","resource":{"@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/15%2F95%2F75%2F159575915627641774730102796320460852675/full/full/0/default.jpg","@type":"dctypes:Image","format":"image/jpeg","height":1650,"width":1275,"service":{"@context":"http://iiif.io/api/image/2/context.json","@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/15%2F95%2F75%2F159575915627641774730102796320460852675","profile":"http://iiif.io/api/image/2/level2.json"}},"on":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/canvas/page-1.json"}]}]}]}