Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of
amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since …

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 …

Amyloid peptides (AMYs) and antimicrobial peptides (AMPs) are considered as the two
distinct families of peptides, characterized by their unique sequences, structures, biological …

Many globular and natively disordered proteins can convert into amyloid fibrils. These fibrils
are associated with numerous pathologies as well as with normal cellular functions,, and …

Several lines of evidence indicate that prefibrillar assemblies of amyloid-β (Aβ)
polypeptides, such as soluble oligomers or protofibrils, rather than mature, end-stage …

Protein aggregation can lead to major disturbances of cellular processes and is associated
with several diseases. We report kinetic and equilibrium data by ThT fluorescence and …

The chemistry of Alzheimer’s disease - Chemical Society Reviews (RSC Publishing) DOI:10.1039/B807980N
Royal Society of Chemistry View PDF VersionPrevious ArticleNext Article DOI: 10.1039/B807980N …

The amyloid fibrils of beta-amyloid (Aβ) peptides play important roles in the pathology of
Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on …

A number of small organic molecules have been developed that bind to amyloid fibrils, a
subset of which also inhibit fibrillization. Among these, the benzothiol dye Thioflavin-T (ThT) …