β-sheet protein aggregate (None in standard usage)

β-sheet protein aggregates are assemblies of misfolded proteins characterized by an extensive β-sheet structure, where β-strands run perpendicular to the fiber axis and are stabilized by interstrand hydrogen bonds. These aggregates are insoluble, highly stable, and resistant to degradation, forming fibrillar deposits known as amyloid. Formation typically occurs due to improper protein folding, mutations, or chemical modifications, and is associated with cytotoxicity and cell stress. β-sheet aggregates serve as pathological markers and therapeutic targets in diseases such as Alzheimer's, Parkinson's, and systemic amyloidoses. They are not unique molecular entities but represent a common structural motif in disease-related protein aggregation.

Other names

Amyloid fibrilscross-β aggregatesprotein amyloidmisfolded β-sheet aggregateamyloid protein aggregate

Antibodies/binders that promote clearance of aggregates Small molecules that inhibit aggregation or promote disaggregation Stabilization of native protein conformation to prevent misfolding Inhibition of nucleation/elongation of fibrils