Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …

Amyloids are a broad class of proteins and peptides that can misfold and assemble into long
unbranched fibrils with a cross-β conformation. These misfolding and aggregation events …

Disorders characterized by α-synuclein (α-syn) accumulation, Lewy body formation and
parkinsonism (and in some cases dementia) are collectively known as Lewy body diseases …

Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While
concerns have recently been raised about its use as a probe specific for amyloid, ThT still …

Abstract The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils
and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Alzheimer's disease is the most fatal neurodegenerative disorder wherein the process of
amyloid-β (Aβ) amyloidogenesis appears causative. Here, we present the 3D structure of the …

To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free
interface. This paper demonstrates the interface between graphene and pure water (verified …

Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various
neurodegenerative diseases. This process involves protein assembly into oligomeric …

Self-assembly processes resulting in linear structures are often observed in molecular
biology, and include the formation of functional filaments such as actin and tubulin, as well …