Open Access. Powered by Scholars. Published by Universities.®
Physical Sciences and Mathematics Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 3 of 3
Full-Text Articles in Physical Sciences and Mathematics
Role Of Aromatic Pi-Stacking On The Aggregation Of Human Islet Amyloid Polypeptide (Hiapp), Srikanth Reddy Konda
Role Of Aromatic Pi-Stacking On The Aggregation Of Human Islet Amyloid Polypeptide (Hiapp), Srikanth Reddy Konda
Master's Theses and Doctoral Dissertations
Human islet amyloid polypeptide (hIAPP) is secreted in the β-cells of the pancreas, which also secretes insulin. In type 2 diabetes mellitus, hIAPP undergoes self-aggregation, forming fibrils. This self-aggregation is cytotoxic and is thought to be linked to type 2 diabetes mellitus by causing β-cell membrane destruction. The N-terminus of hIAPP (1-19) contains a binding site (residues 14-18) for self-aggregation. Aggregation is thought to be mediated by pistacking interactions between phenylalanine residues of hIAPP. In this study, the hIAPP 1-19 sequence was modified by replacing phenylalanine with alanine and naphthylalanine, to study if the modification of the aromatic side chain …
Insulin Based Inhibitors Of Human Islet Amyloid Polypeptide (Hiapp) And Their Effect On Hiapp- Mediated Membrane Damage In Type 2 Diabetes Mellitus, Durgaprasad Peddi
Insulin Based Inhibitors Of Human Islet Amyloid Polypeptide (Hiapp) And Their Effect On Hiapp- Mediated Membrane Damage In Type 2 Diabetes Mellitus, Durgaprasad Peddi
Master's Theses and Doctoral Dissertations
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.
Synthesis And Dye Leakage Assay Of Human And Rat Islet Amyloid Polypeptide 10-19 And Insulin 14-18, Andrew William Gray
Synthesis And Dye Leakage Assay Of Human And Rat Islet Amyloid Polypeptide 10-19 And Insulin 14-18, Andrew William Gray
Master's Theses and Doctoral Dissertations
Islet amylin polypeptide (IAPP) is co-secreted along with insulin in the pancreatic islets of Langerhans. During type 2 diabetes mellitus, human IAPP (hIAPP) fibrilizes to form amyloid deposits that are found post-mortem in more than 95% of people with the disease. Rodents do not suffer from type 2 diabetes mellitus as their IAPP (rIAPP) does not undergo self-aggregation. Although the amyloid deposit is found in those with the disease, the actual cause of the disease is the cytotoxicity of the mechanism that forms those amyloid deposits. The self-aggregation of IAPP to form amyloid deposits is inhibited by insulin due to …