The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …

The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are
the main peptide or protein component of amyloid that develops in the pancreas of type 2 …

With increasing structural information on proteins, the opportunity to understand physical
forces governing protein folding is also expanding. One of the significant non‐covalent …

Amphipathic peptides composed of alternating polar and nonpolar residues have a strong
tendency to self‐assemble into one‐dimensional, amyloid‐like fibril structures. Fibrils …

Amyloid-like fibrous crystals formed by the peptide KFFEAAAKKFFE have been previously
characterized and provide an ideal model system to examine the importance of specific …

Human Islet amyloid polypeptide (hIAPP) from pancreatic β cells in the islet of Langerhans
has different physiological functions including inhibiting the release of insulin and glucagon …

Islet amyloidosis by IAPP contributes to pancreatic β-cell death in diabetes, but the nature of
toxic IAPP species remains elusive. Using concurrent time-resolved biophysical and …

Pancreatic islet amyloid is a characteristic feature of type 2 diabetes. The major protein
component of islet amyloid is the polypeptide hormone known as islet amyloid polypeptide …

Peptide self-assembly leading to cross-β amyloid structures is a widely studied
phenomenon because of its role in amyloid pathology and the exploitation of amyloid as a …