Conditions including heating mode, time, temperature, pH, moisture and protein
concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes …

The formation of amyloid fibrils is critical for neurodegenerative diseases. Some
physiochemical conditions can promote the conversion of proteins from soluble globular …

The misfolding of proteins can lead to fibrillar and non-fibrillar deposits that are the hallmark
of numerous human diseases. Inhibition of protein aggregation is considered as a promising …

In vitro fibrillation of hen egg white lysozyme (HEWL) causes complete reduction of Cu (II) to
Cu (I) at pH 7. Here in the present article, we have shown the presence of both Cu (II) and …

Succinimide intermediates play the crucial role in the nucleation process for protein amyloid
fibril formation, as they can usually induce a non-native conformation in a fraction of soluble …

Comparing higher order structure (HOS) in therapeutic proteins is a significant challenge.
Previously, we showed that changes in solution conditions produced detectable changes in …

Understanding the influence of nanoparticles on the formation of protein amyloid fibrillation
is crucial to extend their application in related biological diagnosis and nanomedicines. In …

We investigated the mechanisms of amyloidlike aggregation and gel formation in hen egg-
white lysozyme (HEWL) in a mixed solvent comprising 90% v/v ethanol in water using …

Amyloid-like fibrils are ordered protein aggregates formed by moderate heating under acidic
conditions. In order to implement them in the food industry, more knowledge has been …

Abstract Kenana Al Adem,“Linking Type 2 Diabetes and Alzheimer's Disease: The Inhibition
of the Cytotoxic IAPP and Aβ Proteins Self-and Co-Aggregation by Small Molecules”, PhD …