Disaggregation of Aβ42 for Structural and Biochemical Studies

Methods Mol Biol. 2018:1777:321-330. doi: 10.1007/978-1-4939-7811-3_20.

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: Alzheimer’s disease; Aβ peptides; Aβ40; Aβ42; FTIR; NMR.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amyloid / chemistry
  • Amyloid beta-Peptides / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Structure*
  • Protein Aggregates*
  • Protein Stability
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Amyloid
  • Amyloid beta-Peptides
  • Protein Aggregates