Amyloid fibril deposit

Amyloid fibril deposits are abnormal extracellular accumulations of highly ordered protein aggregates, characterized by a fibrillar morphology and a cross-β sheet structure[1][5]. They are formed when normally soluble proteins misfold and aggregate into insoluble fibers resistant to degradation, disrupting tissue structure and function[1][2][3]. Amyloid fibril deposits are not a canonical therapeutic target such as a receptor or enzyme, but rather the pathogenic consequence of several protein misfolding disorders (collectively, amyloidoses), including Alzheimer's disease (brain amyloid plaques), systemic AL and AA amyloidosis (multiple organs), and others[1][2]. The specific protein forming amyloid varies by disease, with examples including amyloid-β in Alzheimer's disease, immunoglobulin light chain (AL amyloid) in plasma cell disorders, and transthyretin (ATTR) in hereditary amyloidosis[2][4]. Therapies aim to inhibit the production or aggregation of the precursor protein, stabilize its native form, or promote clearance of deposits, but the deposits themselves are not molecular entities amenable to direct targeting in the way receptor proteins are[1][2][4].

Other names

Amyloid depositsAmyloidAmyloid aggregatesAmyloid plaques

Inhibition of precursor protein production; Promotion of amyloid clearance or breakdown; Stabilization of native protein to prevent misfolding