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β-Amyloid (31-35) is the shortest sequence of native Amyloid-β peptide that retains neurotoxic activity.

β-Amyloid (31-35) is a functional cytotoxic domain of Aβ peptide. β-Amyloid (31-35) increases the phosphorylation of biotinylated Aβ(1-40), enhances CDK-1 activity, and also inhibits binding of Aβ to cyclin B1. β-Amyloid (31-35) is cytotoxic, and such an effect can be inhibited by olomoucine in differentiated human teratocarcinoma cell line, Ntera 2/cl-D1 (NT-2) neurons[1]. β-Amyloid (31-35) shows cytotoxic effect on cerebellar granule cells (CGC). β-Amyloid (31-35) also increases caspase-3 activity in a time-dependent manner (4-24 h) at 40 μM[2].

[1]. Milton NG, et al. The amyloid-beta peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity. Neurosci Lett. 2002 Apr 5;322(2):131-3. [2]. Misiti F, et al. Fragment 31-35 of beta-amyloid peptide induces neurodegeneration in rat cerebellar granule cells via bax gene expression and caspase-3 activation. A crucial role for the redox state of methionine-35 residue. Neurochem Int. 2006 Oct;49(5):525-32.

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