Amylin (Islet Amyloid Polypeptide, IAPP) is a 37 amino acid polypeptide, co-secreted with insulin from pancreatic beta cells, that plays a role in the damage of cell membranes by forming amyloid fibrils in Type 2 diabetes. Insulin has been found to inhibit hIAPP (Human Islet Amyloid Polypeptide) aggregation. The HLVEALYLVC amino acid region of insulin contacts hIAPP near the N-terminus. Truncated and modified analogs of insulin containing the binding region (VEALYLV, VEALFLV and EALYLV) were synthesized and purified, and their actions were studied on model lipid membranes in the presence of hIAPP 1-19 and hIAPP 1-37.
","abstract_html":"<p>Amylin (Islet Amyloid Polypeptide, IAPP) is a 37 amino acid polypeptide, co-secreted with insulin from pancreatic beta cells, that plays a role in the damage of cell membranes by forming amyloid fibrils in Type 2 diabetes. Insulin has been found to inhibit hIAPP (Human Islet Amyloid Polypeptide) aggregation. The HLVEALYLVC amino acid region of insulin contacts hIAPP near the N-terminus. Truncated and modified analogs of insulin containing the binding region (VEALYLV, VEALFLV and EALYLV) were synthesized and purified, and their actions were studied on model lipid membranes in the presence of hIAPP 1-19 and hIAPP 1-37.</p>","abstract_has_math":false,"creators":["Peddi, Durgaprasad"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Dr. Deborah Heyl-Clegg, PhD, Chair"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2009,"date_issued":"2009-01-01T08:00:00Z","date_published":"2009-01-01T08:00:00Z","updated_at":"2026-07-24T02:16:36Z","subjects":["Amylin Research","Amyloid Research","Peptides Research","Diabetes Research","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/261","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dr. Deborah Heyl-Clegg, PhD, Chair"]},{"key":"dc:creator","label":"Author","values":["Peddi, Durgaprasad"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"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":["Amylin Research","Amyloid Research","Peptides Research","Diabetes Research","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/261"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Amylin (Islet Amyloid Polypeptide, IAPP) is a 37 amino acid polypeptide, co-secreted with insulin from pancreatic beta cells, that plays a role in the damage of cell membranes by forming amyloid fibrils in Type 2 diabetes. Insulin has been found to inhibit hIAPP (Human Islet Amyloid Polypeptide) aggregation. The HLVEALYLVC amino acid region of insulin contacts hIAPP near the N-terminus. Truncated and modified analogs of insulin containing the binding region (VEALYLV, VEALFLV and EALYLV) were synthesized and purified, and their actions were studied on model lipid membranes in the presence of hIAPP 1-19 and hIAPP 1-37.
"]},{"key":"dc:title","label":"Title","values":["Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on hIAPP- mediated membrane damage in type 2 diabetes mellitus"]}]}],"canonical_facts":{"dc:contributor":["Dr. Deborah Heyl-Clegg, PhD, Chair"],"dc:creator":["Peddi, Durgaprasad"],"dc:description.abstract":["Amylin (Islet Amyloid Polypeptide, IAPP) is a 37 amino acid polypeptide, co-secreted with insulin from pancreatic beta cells, that plays a role in the damage of cell membranes by forming amyloid fibrils in Type 2 diabetes. Insulin has been found to inhibit hIAPP (Human Islet Amyloid Polypeptide) aggregation. The HLVEALYLVC amino acid region of insulin contacts hIAPP near the N-terminus. Truncated and modified analogs of insulin containing the binding region (VEALYLV, VEALFLV and EALYLV) were synthesized and purified, and their actions were studied on model lipid membranes in the presence of hIAPP 1-19 and hIAPP 1-37.
"],"dc:identifier":["https://commons.emich.edu/theses/261"],"dc:subject":["Amylin Research","Amyloid Research","Peptides Research","Diabetes Research","Chemistry"],"dc:title":["Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on hIAPP- mediated membrane damage in type 2 diabetes mellitus"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:36Z"}