Date Approved
2011
Degree Type
Open Access Thesis
Degree Name
Master of Science (MS)
Department or School
Chemistry
Committee Member
Deborah Heyl-Clegg, PhD, Chair
Committee Member
Dr. Hedeel Evans, PhD
Committee Member
Dr. Maria Milletti, PhD
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.
Recommended Citation
Pesaru, Ranadheer R., "Insulin based inhibitors of human islet amyloid polypeptide (hIAPP) and their effect on aggregation of hIAPP in the treatment of type II diabetes" (2011). Master's Theses and Doctoral Dissertations. 336.
https://commons.emich.edu/theses/336