Amyloid beta 25–35 peptide (Aβ(25–35))

Amyloid beta 25–35 peptide (Aβ(25–35)) is a synthetic 11-amino acid fragment of the amyloid beta protein sequence found in Alzheimer’s disease plaques. Its sequence is NH₂–Gly–Ser–Asn–Lys–Gly–Ala–Ile–Ile–Gly–Leu–Met–COOH, corresponding to amino acids 25 to 35 of the amyloid precursor protein-derived amyloid-beta peptide[5]. Despite being much shorter than the full-length Aβ(1–40/42), Aβ(25–35) retains the toxic, aggregating, and neurodegenerative properties of the parent peptides and is the shortest fragment that can still form toxic amyloid fibrils[1][5][6]. Widely used in experimental models of Alzheimer’s disease, Aβ(25–35) rapidly induces apoptotic cell death, oxidative stress, intracellular calcium overload, disruption of neuronal gene expression, and other hallmarks of AD-related neurotoxicity in vitro and in vivo[1][2][3][5][6][7]. Aβ(25–35) itself is a target for aggregation inhibition by small molecule drugs in research settings, with molecules such as myricetin, curcumin, and tetracycline shown to interfere with its fibril formation and toxicity[1]. Although this fragment is not detected as a major species in human AD plaques, it is a widely used research tool to explore amyloid toxicity and to screen potential anti-amyloid therapeutics, rather than a distinct therapeutic target in clinical development.

Other names

Amyloid β 25–35Beta-amyloid 25–35Abeta(25–35)Aβ(25–35) peptideβ-Amyloid (25–35)

Inhibition of peptide self-assembly (aggregation inhibitors bind to Aβ(25–35) and prevent β-sheet/fibril formation)[1] Antioxidant-mediated reduction of peptide-induced oxidative stress[3] Immunotherapeutic clearance of Aβ species (for full length peptides and by some cross-reactivity, though not specifically established for Aβ(25–35))[4]