Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While
concerns have recently been raised about its use as a probe specific for amyloid, ThT still …

Many proteins exert their biological activities through small exposed surface regions called
epitopes that are folded peptides of well‐defined three‐dimensional structures. Short …

The aggregation of proteins is tightly controlled in living systems, and misfolded proteins are
normally removed before aggregation of the misfolded protein can occur. But for reasons not …

The purpose of this work was to construct a consensus prediction algorithm of 'aggregation-
prone'peptides in globular proteins, combining existing tools. This allows comparison of the …

This tutorial review presents descriptions of two amyloidogenic proteins, amyloid-β (Aβ)
peptides and islet amyloid polypeptide (IAPP), whose misfolding propensities are implicated …

Bacterial biofilms are highly structured multicellular communities whose formation involves
flagella and an extracellular matrix of adhesins, amyloid fibers, and exopolysaccharides …

In the history of science and technology, researchers have always undertaken endeavors to
enhance the degree of “directness of measurement”. With “directness of measurement”, we …

Due to the high aspect ratio, appealing mechanical characteristics, and various adjustable
functional groups on the surface proteins, food‐grade protein nanofibrils have attracted …

Human islet amyloid polypeptide is a hormone coexpressed with insulin by pancreatic beta-
cells. For reasons not clearly understood, hIAPP aggregates in type II diabetics to form …

To control and enhance protein functionality is a major challenge for food scientists. In this
context, research on food protein fibril formation, especially amyloid fibril formation, holds …