title: Analysis of Abeta interactions using ProteinChip technology.
abstract: Abeta peptides are now acknowledged to play a central role in the pathogenesis of Alzheimer's disease. Their generation results from the sequential cleavage of amyloid precursor protein by beta and gamma secretases. The resulting peptide fragments impart toxicity via their ability to form soluble oligomers and bind to cell membranes. In this chapter we describe the use of ProteinChip technology to study the physicochemical behaviour of Abeta and its mechanisms of toxicity. These include analyzing (1) Abeta processing and quantitation of peptide fragments, (2) Abeta aggregation and the quantitation of oligomers, and (3) Abeta-lipid interactions.
authors: Howard Florey Institute, University of Melbourne, Parkville, Victoria, Australia.
authors: Eleni
authors: E
authors: Giannakis
authors: Lin-Wai
authors: LW
authors: Hung
authors: Keyla Perez
authors: KP
authors: Camacaro
authors: David P
authors: DP
authors: Smith
authors: Kevin J
authors: KJ
authors: Barnham
authors: John D
authors: JD
authors: Wade
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D040081:Protein Array Analysis / Q000295:instrumentation / Q000379:methods
chemical_list: D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D010446:Peptide Fragments