Amyloid is an abnormal extracellular fibrillar protein deposit in the tissues. In humans, more
than 25 different proteins can adopt a fibrillar conformation in vivo that results in the …

Neurodegenerative disorders, such as Alzheimer's, Parkinson's, and prion diseases, are
directly linked to the formation and accumulation of protein aggregates in the brain. These …

The aggregation of the natively disordered protein, Tau, to form lesions called neurofibrillary
tangles is a characteristic feature of several neurodegenerative tauopathies. The polyanion …

Aggregation of the amyloid-β (Aβ) peptide is strongly correlated with Alzheimer's disease
(AD). Recent research has improved our understanding of the kinetics of amyloid fibril …

Primary light chain amyloidosis is the most common form of systemic amyloidosis and is
caused by misfolded light chains that cause proteotoxicity and rapid decline of vital organ …

Different proteins have different amino acid sequences as well as conformations, and
therefore different propensities to aggregate. Electrostatic interactions have an important …

Monomeric and aggregated states of an IgG1 antibody were characterized under acidic
conditions as a function of solution pH (3.5–5.5). A combination of intrinsic/extrinsic …

Amyloid cascades leading to peptide β-sheet fibrils and plaques are central to many
important diseases. Recently, intermediate assemblies of these cascades were identified as …

Glycosaminoglycans (GAGs), which are found in association with all extracellular amyloid
deposits in humans, are known to accelerate the aggregation of various amyloidogenic …

Electrostatic and hydrophobic interactions have an important role in the protein aggregation.
In this study, we have investigated the effect of charge and hydrophobicity of oppositely …