Quantitative understanding of the kinetics of fibril formation and the molecular mechanism of
transition from monomers to fibrils is needed to obtain insights into the growth of amyloid …

The aggregation of soluble proteins into fibrillar species is a complex process that spans
many lengths and time scales, and that involves the formation of numerous on-pathway and …

In situ and real-time characterization of protein secondary structures at interfaces is
important in biological and bioengineering sciences, yet remains technically challenging. In …

Early oligomerization of human IAPP (hIAPP) is responsible for β-cell death in the pancreas
and is increasingly considered a primary pathological process linked to Type II Diabetes …

The advent of laser-based sources of ultrafast infrared pulses has extended the study of very
fast molecular dynamics to the observation of processes manifested through their effects on …

Amyloid formation has been implicated in the pathology of over 20 human diseases, but the
rational design of amyloid inhibitors is hampered by a lack of structural information about …

Infrared (IR) spectroscopy of the amide I band has been widely utilized for the analysis of
peptides and proteins. Theoretical modeling of IR spectra of proteins requires an accurate …

This Perspective highlights recent computational approaches to protein aggregation, from
coarse-grained models to atomistic simulations, using the islet amyloid polypeptide (IAPP) …

The aggregation of human amylin to form amyloid contributes to islet β-cell dysfunction in
type 2 diabetes. Studies of amyloid formation have been hindered by the low structural …

Patients with type II diabetes exhibit fibrillar deposits of human amylin protein in the
pancreas. It has been proposed that amylin oligomers arising along the aggregation or fibril …