Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

The self-assembly of proteins is an essential process for a variety of cellular functions
including cell respiration, mobility and division. On the other hand, protein or peptide …

The thermodynamic hypothesis of protein folding, known as the “Anfinsen's dogma” states
that the native structure of a protein represents a free energy minimum determined by the …

Light chain (AL) amyloidosis is a debilitating disease in which mutant antibody light chains
(LC), secreted by aberrant plasma cell clones, misfold and form insoluble fibrils, which can …

Abstract β2-microglobulin (β2m) and its truncated variant ΔΝ6 are co-deposited in amyloid
fibrils in the joints, causing the disorder dialysis-related amyloidosis (DRA). Point mutations …

From a physicochemical viewpoint, amyloid fibril formation is a phase transition from soluble
to crystal-like sates limited by supersaturation. It occurs only above solubility (ie, the …

Polyphosphate (polyP), which is found in various microorganisms and human cells, is an
anionic biopolymer consisting of inorganic phosphates linked by high-energy phosphate …

Ultrasonication has been recently adopted in amyloid-fibril assays because of its ability to
accelerate fibril formation, being promising in the early stage diagnosis of amyloidoses in …

Caseins are a diverse family of intrinsically disordered proteins present in the milks of all
mammals. A property common to two cow paralogues, α S2-and κ-casein, is their propensity …