Beta Amyloid Fibril (None)

Beta amyloid fibrils are insoluble, fibrous protein aggregates formed by the self-assembly of amyloid beta (Aβ) peptides. These fibrils are a hallmark of Alzheimer's disease pathology and are found in the extracellular plaques characteristic of the disorder. The formation and accumulation of beta amyloid fibrils are closely linked to neurodegeneration and cell death in Alzheimer's disease. The fundamental structural motif is the cross-β structure, where β-strands run perpendicular to the long axis of the fibril, forming extended β-sheets that stack parallel to each other along the fiber axis. Fibrils consist of several protofilaments, which laterally associate into mature fibers. In Aβ(1–42) fibrils, residues 18–42 form a β-strand–turn–β-strand motif with two intermolecular, parallel, in-register β-sheets. Residues 1–17 remain disordered. Amyloid beta peptides range from 36–43 amino acids; Aβ(1–40) and Aβ(1–42) are most common in human pathology.

Other names

Amyloid beta fibrilAβ fibrilAmyloid plaque

Aggregation inhibition (potential)