Ping Cao

TL;DR: 2D infrared spectroscopy and isotope labeling are used to monitor the kinetics of fibril formation by human islet amyloid polypeptide (hIAPP or amylin) that is associated with type 2 diabetes and find that an oligomeric intermediate forms during the lag phase with parallel β-sheet structure in a region that is ultimately a partially disordered loop in the fibrils.

TL;DR: Open questions in the field include the relative importance of the various mechanisms of β-cell death, the relevance of reductionist biophysical studies to the situation in vivo, the molecular mechanism of amyloid formation in vitro and in vivo; and the design of soluble, bioactive variants of IAPP for use as adjuncts to insulin therapy.

TL;DR: It is shown that the polyphenolic compounds epigallocatechin gallate and silibinin bind to specific conformers within a dynamic ensemble of hIAPP monomers, altering the progress of oligomerization and fibril assembly.

TL;DR: Islet amyloid is not the cause of type 2 diabetes, but it leads to β‐cell dysfunction and cell death, and contributes to the failure of islet cell transplantation.

TL;DR: This work uses isotope labeling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin, the peptide responsible for islet amyloid formation in type 2 diabetes, with a known inhibitor, rat amyl in.