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Quantifying the Aggregation Propensity of IAPP from Diabetic and Nondiabetic Species
Author(s) -
Moffet David,
Palato Larry,
Pilcher Shan,
Rinauro Dillon,
Menefee Kate,
Tun Angela,
Jauregui Betssy,
Shapiro Sarah,
Nossiff Olivia,
Nguyen Viviane
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.795.6
Subject(s) - amylin , amyloid (mycology) , islet , protein aggregation , diabetes mellitus , peptide , chemistry , biochemistry , biology , computational biology , endocrinology , inorganic chemistry
The aggregation of the 37‐amino acid polypeptide human Islet Amyloid Polypeptide (hIAPP, amylin), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of pancreatic β‐islet cells in type 2 diabetes. It is known that several organisms express non‐amyloidogenic variants of IAPP (such as rat and mouse) and are not known to develop diabetes naturally. Conversely, several organisms express highly amyloidogenic variants of IAPP (such as human, cat and primates) and are known to develop diabetes. Despite the significant amount of genetic information available, no comprehensive study has been conducted to directly correlate IAPP aggregation potential to the propensity to develop diabetes within the animal kingdom. In this work, we will compare the aggregation potential of naturally occurring IAPP variants from organisms known to, or known not to, develop diabetes. IAPP peptide variants were chemically synthesized. Each variant was tested for its amyloid aggregation potential using Circular Dichroism and Atomic Force Microscopy. Support or Funding Information National Institute of Health (Grant#: 1R15DK112172) This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .