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Disaggregation of Aβ42 for Structural and Biochemical Studies.

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The amyloid-β (Aβ) peptides that form the amyloid fibrils associated with Alzheimer's disease are generated by sequential proteolysis of the amyloid precursor protein by β- and γ-secretase. The two predominant… Click to show full abstract

The amyloid-β (Aβ) peptides that form the amyloid fibrils associated with Alzheimer's disease are generated by sequential proteolysis of the amyloid precursor protein by β- and γ-secretase. The two predominant Aβ peptides, Aβ40 and Aβ42, differ by two amino acids, are soluble as monomers at low concentration (and/or low temperature) and are normally cleared from the brain parenchyma. In order to study the structure and assembly of these peptides, they are often synthesized using solid-phase peptide synthesis and purified. Here, we outline the method we use to prepare monomeric Aβ for structural and biochemical studies.

Keywords: disaggregation structural; biochemical studies; biology; structural biochemical

Journal Title: Methods in molecular biology
Year Published: 2018

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