Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta cells in the pancreas of type II diabetic patients. The presence of amyloid deposits is also a characteristic feature of a number of other diseases like Alzheimer’s disease and Parkinson’s disease. Since insulin has been reported to interact with hIAPP and block amyloid formation, fragments of insulin were synthesized and the inhibitory effects were studied against an hIAPP analog in the presence of phospholipid vesicles. While these sequences might inhibit amyloid formation, preliminary results indicate that they actually enhance membrane damage, as measured by the increased leakage of carboxyfluoroscein dye from membrane model vesicles.
","abstract_html":"<p>Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta cells in the pancreas of type II diabetic patients. The presence of amyloid deposits is also a characteristic feature of a number of other diseases like Alzheimer’s disease and Parkinson’s disease. Since insulin has been reported to interact with hIAPP and block amyloid formation, fragments of insulin were synthesized and the inhibitory effects were studied against an hIAPP analog in the presence of phospholipid vesicles. While these sequences might inhibit amyloid formation, preliminary results indicate that they actually enhance membrane damage, as measured by the increased leakage of carboxyfluoroscein dye from membrane model vesicles.</p>","abstract_has_math":false,"creators":["Pesaru, Ranadheer R."],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Deborah Heyl-Clegg, PhD, Chair","Dr. Hedeel Evans, PhD","Dr. Maria Milletti, PhD"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-01-01T08:00:00Z","date_published":"2011-01-01T08:00:00Z","updated_at":"2026-07-24T02:16:44Z","subjects":["insulin","inhibitors","diabetes","hIAPP","membrane","damage","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/336","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Deborah Heyl-Clegg, PhD, Chair","Dr. Hedeel Evans, PhD","Dr. Maria Milletti, PhD"]},{"key":"dc:creator","label":"Author","values":["Pesaru, Ranadheer R."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2011-09-15T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Open Access Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["insulin","inhibitors","diabetes","hIAPP","membrane","damage","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/336"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta cells in the pancreas of type II diabetic patients. The presence of amyloid deposits is also a characteristic feature of a number of other diseases like Alzheimer’s disease and Parkinson’s disease. Since insulin has been reported to interact with hIAPP and block amyloid formation, fragments of insulin were synthesized and the inhibitory effects were studied against an hIAPP analog in the presence of phospholipid vesicles. While these sequences might inhibit amyloid formation, preliminary results indicate that they actually enhance membrane damage, as measured by the increased leakage of carboxyfluoroscein dye from membrane model vesicles.
"]},{"key":"dc:title","label":"Title","values":["Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes"]}]}],"canonical_facts":{"dc:contributor":["Deborah Heyl-Clegg, PhD, Chair","Dr. Hedeel Evans, PhD","Dr. Maria Milletti, PhD"],"dc:creator":["Pesaru, Ranadheer R."],"dc:date.available":["2011-09-15T07:00:00Z"],"dc:description.abstract":["Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta cells in the pancreas of type II diabetic patients. The presence of amyloid deposits is also a characteristic feature of a number of other diseases like Alzheimer’s disease and Parkinson’s disease. Since insulin has been reported to interact with hIAPP and block amyloid formation, fragments of insulin were synthesized and the inhibitory effects were studied against an hIAPP analog in the presence of phospholipid vesicles. While these sequences might inhibit amyloid formation, preliminary results indicate that they actually enhance membrane damage, as measured by the increased leakage of carboxyfluoroscein dye from membrane model vesicles.
"],"dc:identifier":["https://commons.emich.edu/theses/336"],"dc:subject":["insulin","inhibitors","diabetes","hIAPP","membrane","damage","Chemistry"],"dc:title":["Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:44Z"}