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Ab is a proteolytic product of the large Type I membrane protein, amyloid precursor protein (APP). Two proteases, memapsin 2 (b-secretase) and g-secretase, are involved in the cleavage of b-amyloid precursor protein to form b-amyloid peptide (Ab). Amyloid plaques (Ab) are primarily composed of the toxic Ab (1-42 peptide) and their accumulation leads to the progression of Alzheimer’s disease (AD). In the case of early on-set familial AD (FAD), gene mutations in three genes (APP, PS1, and PS2) are responsible for increasing synthesis of Ab (1-42). It is believed that strategies to lower the concentration of Ab in the brain should prove beneficial for future therapeutic approaches in the treatment of AD. The b-site APP cleaving enzyme (BACE1 aka Memapsin 2 and Asp2) was identified in 1999 by Vassar et al. as a novel transmembrane aspartyl protease possessing b-secretase activity (1). A new fluorescence resonance energy transfer (FRET) peptide substrate (SFQ-3690-PI), derived from the sequence (EVNLDAEF) found in the b-secretase site of the Swedish mutation of Amyloid Precursor Protein (APP), was reported by Ermolieff et al. (2). This new fluorogenic substrate is now available from Peptides International as a research tool to aid Alzheimer’s disease research efforts. |
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2. J. Ermolieff, J.A. Loy, G. Koelsch, and J. Tang, Biochemistry 39, 12450 (2000). |
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