Disaggregation of Aβ42 for Structural and Biochemical Studies

  • Hyewon Chung
  • Elliot J. Crooks
  • Martine Ziliox
  • Steven O. Smith
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1777)

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.

Key words

Aβ peptides Aβ40 Aβ42 Alzheimer’s disease FTIR NMR 

Notes

Acknowledgments

This work was supported by NIH-NSF instrumentation grants (S10 RR13889 and DBI-9977553), a grant from the NIH to S.O.S (AG 27317). We gratefully acknowledge the W.M. Keck Foundation for support of the NMR facilities in the Center of Structural Biology at Stony Brook.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • Hyewon Chung
    • 1
  • Elliot J. Crooks
    • 2
  • Martine Ziliox
    • 2
  • Steven O. Smith
    • 2
  1. 1.Department of OphthalmologyKonkuk University Medical Center, Konkuk University School of MedicineSeoulSouth Korea
  2. 2.Department of Biochemistry and Cell BiologyStony Brook UniversityStony BrookUSA

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