Amyloid beta Peptide

Literature References: A 39-43 residue peptide deposited into the extracellular amyloid or senile plaques characterizing Alzheimer's disease and Down's syndrome. Mol wt approx 4,200. Multiple isoforms exist, the most predominant are 40 and 42 amino acids in length. Natural component of cerebrospinal fluid and blood plasma; sol under normal conditions. Forms insol, cytotoxic fibrillar plaques and aggregates in diseased brains. Derived from the proteolysis of amyloid precursor protein by proteases known as secretases. Purification and characterization: G. G. Glenner, C. W. Wong, Biochem. Biophys. Res. Commun. 120, 885 (1984); C. L. Masters et al., Proc. Natl. Acad. Sci. USA 82, 4245 (1985). Structure and neurotoxicity studies: L. K. Simmons et al., Mol. Pharmacol. 45, 373 (1994); C. J. Pike et al., J. Neurochem. 64, 253 (1995). Brain accumulation of Ab during aging and in Alzheimer's disease: H. Funato et al., Am. J. Pathol. 152, 1633 (1998). Role of soluble oligomers in Alzheimer's disease: R. Kayed et al., Science 300, 486 (2003). Soly study of Ab40: P. Sengupta et al., Biochemistry 42, 10506 (2003). Oligomerization study: G. Bitan et al., J. Biol. Chem. 278, 34882 (2003). Clinical evaluation of immunization with aggregated Ab42 in Alzheimer's disease: C. Hock et al., Neuron 38, 547 (2003). Series of articles: J. Struct. Biol. 130, 87-371 (2000). Review of solid state NMR studies: R. Tycko, Biochemistry 42, 3151-3159 (2003). Reviews of role in Alzheimer's disease: C. L. Joachim, D. J. Selkoe, Alzheimer Dis. Assoc. Disord. 6, 7-34 (1992). D. H. Small, C. A. McLean, J. Neurochem. 73, 443-449 (1999); D. A. Butterfield et al., Trends Mol. Med. 7, 548-554 (2001); W. I. Rosenblum, Neurobiol. Aging 23, 225-230 (2002); T. E. Golde et al., Biochim. Biophys. Acta 1502, 172-187 (2002).