Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …

Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review
the impact of various conditions and food constituents on amyloid fibrillation of milk and …

Protein-based amyloid fibrils can show a great variety of polymorphic structures within the
same protein precursor, although the origins of these structural homologues remain poorly …

Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the
exact role of disulfide bonds in protein aggregation is still not well-understood. The …

Abstract Soymilk (about 3% protein and 1.8% lipids), prepared by wet disintegration of
soaked soybeans, was heated at 108° C for 15 min and then subjected to in vitro gastric …

Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the
organism. Depending on the environment's pH conditions, HSA can take one of the five …

Abstract Changes in pH affect metabolic pathways, primarily by modulating enzyme
conformations, which is why a detailed analysis of pH-driven conformational transitions is …

Depending on external conditions, native proteins may change their structure and undergo
different association routes leading to a large scale polymorphism of the aggregates. This …

Fibrillogenesis of the small peptide Aβ (1–40) is considered to be the hallmark of
Alzheimer's disease. Some evidence indicates small oligomers, rather than mature fibrils, as …

In the current study we have investigated the interaction of newly approved kinase inhibitors
namely Cabozantinib (CBZ) and Tofacitinib (TFB) with human Alpha-1 acid glycoprotein …