Abstract
The amyloid-beta peptide is considered as a key player in the development and progression of Alzheimer’s disease (AD). Although good evidence exists that amyloid-beta accumulates inside cells, intracellular brain amyloid-beta-binding proteins remain poorly characterized. Here we describe a protocol for affinity-based profiling of amyloid-beta-binding proteins of rat brain, their proteomic identification and validation by a surface plasmon resonance (SPR)-based analysis. It includes: (a) SPR-based selection of immobilization conditions for beta-amyloid coupling and choice of appropriate resin for preparation of an affinity sorbent; (b) immobilization of beta-amyloid on the selected resin; (c) preparation of biological samples (rat brain homogenate) for affinity-based separation; (d) isolation of rat brain proteins by affinity chromatography using amyloid-beta as the affinity ligand; (e) sample preparation for proteomic analysis; (f) proteomic analysis and protein identification; (g) SPR-based validation of the interaction of identified proteins with immobilized amyloid-beta.
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Acknowledgments
This work was supported by the Russian Science Foundation (grant no. 14-24-00100) within the project “The role of structural polymorphism of amyloid-beta in initiation of Alzheimer’s disease.”
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Medvedev, A. et al. (2015). Amyloid-Binding Proteins: Affinity-Based Separation, Proteomic Identification, and Optical Biosensor Validation. In: Posch, A. (eds) Proteomic Profiling. Methods in Molecular Biology, vol 1295. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2550-6_33
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DOI: https://doi.org/10.1007/978-1-4939-2550-6_33
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