Alpha-synuclein fibril (α-Syn fibril (or Fibrillar α-Syn))

Fibrillar alpha-synuclein is the aggregated, insoluble amyloid form of the protein alpha-synuclein. In healthy neurons, alpha-synuclein functions in vesicle trafficking and membrane interaction, but its misfolding and assembly into cross-beta sheet-rich fibrils is a key event in the pathogenesis of Parkinson’s disease and other synucleinopathies[2][3][4]. These fibrils accumulate within neuronal inclusions called Lewy bodies, disrupt lysosomal structure and function, induce neurotoxicity, and promote intercellular propagation through direct transfer or via tunneling nanotubes, reflecting a prion-like mechanism[5][7]. Structural studies reveal polymorphic fibril assemblies, often stabilized by hydrophobic interactions and lipid binding, and highlight end-dependent growth mechanisms and the roles of truncated alpha-synuclein species in disease[1][2][4]. This target is not a classical receptor or enzyme, but rather a pathogenic protein aggregate; its aberrant accumulation drives neurodegenerative processes and is the focus of biomarker development and therapeutic intervention[4].

Other names

Alpha-synuclein aggregateAmyloid alpha-synucleinα-Synuclein fibrilFibrillar α-Syn

Inhibition of fibrillization; Disruption or disaggregation of fibrils; Prevention of cell-to-cell propagation; Clearance enhancement by promoting autophagy/lysosomal function; Blockade with anti-α-synuclein antibodies.