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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.