Quantifying the Aggregation Propensity of IAPP from Diabetic and Nondiabetic Species

• DOI: 10.1096/fasebj.2018.32.1_supplement.795.6
• Publication Date: 2021-06-21T14:53:54Z
• Authors: David Moffet; Larry Palato; Shannon Pilcher; Dillon Rinauro; Kate Menefee; Angela Tun; Betssy Jauregui; Sarah Shapiro; Olivia Nossiff; Viviane Nguyen
• Keywords: Amylin; Amyloid (mycology)

The aggregation of the 37‐amino acid polypeptide human Islet Amyloid Polypeptide (hIAPP, amylin), as either insoluble amyloid or small oligomers, appears to play a direct role in death pancreatic β‐islet cells type 2 diabetes. It is known that several organisms express non‐amyloidogenic variants IAPP (such rat and mouse) are not develop diabetes naturally. Conversely, highly amyloidogenic human, cat primates) Despite significant amount genetic information available, no comprehensive study has been conducted directly correlate potential propensity within animal kingdom. In this work, we will compare naturally occurring from to, peptide were chemically synthesized. Each variant was tested for its using Circular Dichroism Atomic Force Microscopy. Support Funding Information National Institute Health (Grant#: 1R15DK112172) This abstract Experimental Biology 2018 Meeting. There full text article associated with published FASEB Journal .