Amyloid-beta 42 peptide (Aβ42)

Amyloid-beta 42 peptide is a **42–amino-acid proteolytic fragment** derived from amyloid precursor protein (APP) via sequential cleavage by β- and γ-secretases[1][2]. Aβ42 is an *intrinsically disordered peptide* in solution that adopts multiple conformations but, upon aggregation, forms beta-sheet-rich oligomers and fibrils that are a **hallmark of Alzheimer's disease (AD)** pathology[1][2][4][9]. Compared to the closely related Aβ40 peptide, Aβ42 is **more prone to aggregation** due to its hydrophobic C-terminus and more structured conformations, leading to the formation of neurotoxic oligomers and amyloid plaques in the brain[1][2][4]. The aggregation of Aβ42 is a central event in the molecular pathogenesis of AD, with both soluble oligomers and insoluble fibrils contributing to synaptic dysfunction and neurodegeneration[2][8][9]. Several **therapeutics targeting Aβ42 clearance or aggregation** have been developed as disease-modifying strategies for Alzheimer's disease, primarily monoclonal antibodies that bind Aβ aggregates and promote their removal[6][9]. Amyloid-beta 42 levels in cerebrospinal fluid and blood, as well as amyloid PET imaging, are widely used as **biomarkers for AD diagnosis and monitoring**[9]. The peptide’s involvement in complex aggregation pathways and its pivotal role as an **AD therapeutic target** make Aβ42 a molecule of major biomedical and clinical significance[1][2][4][9].

Other names

beta-amyloid (1-42)Amyloid β 1-42Beta-amyloid peptide (1-42)β-amyloid 42Aβ(1–42)AN1792HB9805

Antibody-mediated clearance of amyloid plaques; Inhibition of peptide aggregation; Promotion of peptide degradation/clearance