Protein aggregate with repetitive β-sheet structure

A protein aggregate with repetitive β-sheet structure is a supramolecular assembly in which polypeptide chains form extended, hydrogen-bonded β-sheet motifs, often arranged in parallel or antiparallel fashion[4][2][3][6]. These structures are highly ordered and typically stack to form fibrils, as is characteristic in amyloid aggregates. The repetitive cross-β-sheet architecture is stabilized by extensive inter-strand hydrogen bonding, resulting in aggregates that are insoluble and highly resistant to proteolysis[2][4][7]. This configuration is associated with a range of diseases—most notably neurodegenerative disorders (e.g., Alzheimer's, prion diseases), but also with some functional biological roles. Protein aggregation into β-sheet-rich structures is a hallmark of pathological misfolding, driving cellular toxicity by exposing hydrophobic surfaces, sequestering vital cell components, and occasionally by forming pore-like cytotoxic assemblies[5][1][7]. Therapeutic strategies often aim to inhibit the nucleation or propagation of these aggregates, or to promote their clearance by immune or chemical means[5][6][7].\n\nThe term provided is structurally descriptive and aligns with amyloid and prion literature, but is not a canonical protein or gene name used in molecular pharmacology; the more precise target name is amyloid fibril or amyloid β-protein (when discussing Alzheimer's disease)[7][4][5].

Other names

Amyloid fibrilprotein aggregatecross-β-sheet aggregateβ-sheet-rich aggregate

Inhibition of aggregate formation\nDestabilization/disaggregation of β-sheet-rich aggregates\nImmune-mediated clearance (antibody binding and phagocytosis)