Peptide Self-Assembly
Humana Press
Chapter title |
Disaggregation of Aβ42 for Structural and Biochemical Studies
|
---|---|
Book title |
Peptide Self-Assembly
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7811-3_20 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7809-0, 978-1-4939-7811-3
|
Authors |
Hyewon Chung, Elliot J. Crooks, Martine Ziliox, Steven O. Smith |
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. |
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Unknown | 6 | 100% |
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Student > Bachelor | 1 | 17% |
Researcher | 1 | 17% |
Student > Doctoral Student | 1 | 17% |
Unknown | 1 | 17% |
Readers by discipline | Count | As % |
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Chemistry | 2 | 33% |
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Unknown | 1 | 17% |