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Amyloid-β (Aβ) research compounds include Aβ peptides and modulators of Aβ production, aggregation and signaling. Aβ was first purified from cerebrovascular amyloid in Alzheimer's disease and characterized in 1984. The peptide is cleaved from the amyloid precursor protein (APP), whose cloning in 1987 revealed a structure resembling a cell-surface receptor. The amyloid hypothesis proposes that Aβ accumulation drives Alzheimer's disease pathogenesis, and it frames much current research. The category includes Amyloid b-Peptide (1-42) (human) for aggregation and toxicity studies. γ-Secretase inhibitors such as avagacestat and RO4929097 reduce Aβ formation. FPS-ZM1 blocks the receptor for advanced glycation end products (RAGE), which binds Aβ.
Amyloid b-Peptide (10-20) (human), soluble amyloid b-peptide fragment that is a substrate for gelatinase A/type IV collagenase/MMP-2 and APP secretase; cleaved between Lys16 and Leu17.
Mca-SEVKMDAEFRK(Dnp)RR-NH2 is a substrate specifically designed for thimet oligopeptidase (TOP), featuring the beta-secretase cleavage site of the wild-type amyloid precursor protein (APP). This compound plays a crucial role in elucidating the processing of APP and the pathways leading to Alzheimer's disease. It serves as a valuable tool for researchers investigating amyloid pathology and related neurodegenerative processes.
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