In the last century, small-molecule natural products were the main inspiration for most drug
discovery programs based either on high-throughput screening (HTS) or rational design …

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 …

Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical
properties compared to native monomers, but there is as yet insufficient understanding of …

It has been known for many decades that cell surface, soluble-secreted, and extracellular
matrix proteins are generally rich in disulfide bonds, but only more recently has the …

The potential of cold plasma (CP) treatment to promote the formation of amyloid fibrils (AFs)
of ovalbumin (OVA) was evaluated relative to acidic heat fibrillation condition (pH= 2, 85° C) …

Almost all published studies of heat-induced β-lactoglobulin self-assembly into amyloid-like
fibrils at low pH and low ionic strength have involved heating at 80° C, and the effect of …

The bovine whey protein β-lactoglobulin will self-assemble into amyloid-like nanofibrils
when heated at pH≤ 3 and temperatures≥ 75° C. These fibrils have diameters< 10 nm and …

The deposition of proteins in the form of amyloid fibrils is closely associated with several
serious diseases. The events that trigger the conversion from soluble functional proteins into …

High-throughput genomic sequencing has focused attention on understanding differences
between species and between individuals. When this genetic variation affects protein …

Whey proteins, a group of acid-soluble proteins, represent approximately 20% of the total
protein in bovine milk. The two main proteins, β-lactoglobulin (18.3 kDa) and α-lactalbumin …