Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Abnormal aggregation of proteins into filamentous aggregates commonly associates with
many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes …

Amyloid fibers and oligomers are associated with a great variety of human diseases
including Alzheimer's disease and the prion conditions. Here we attempt to connect recent …

Dozens of proteins are known to convert to the aggregated amyloid state. These include
fibrils associated with systemic and neurodegenerative diseases and cancer, functional …

The primary component of the amyloid plaques in Alzheimer's disease (AD) is a highly
ordered fibril composed of the 39− 43 amino acid peptide, β-amyloid (Aβ). The presence of …

Amyloid diseases display the presence, in targeted tissues and organs, of fibrillar deposits of
specific peptides or proteins. Increasing efforts are presently spent in investigating the …

Increasing evidence indicates that oligomeric protein assemblies may represent the
molecular species responsible for cytotoxicity in a range of neurological disorders including …

A detailed understanding of the molecular events underlying the conversion and self-
association of normally soluble proteins into amyloid fibrils is fundamental to the …

Examination of the N‐terminal sequence of non‐Aβ component of Alzheimer's Disease
amyloid (NAC) revealed a degree of similarity to regions crucial for aggregation and toxicity …

Highlights•We review recent drugs mainly targeting Aβ and how they were identified.•We
report their results from in vitro and in vivo experiments and clinical trials.•We describe …