Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods

Methods Mol Biol. 2018:1777:331-338. doi: 10.1007/978-1-4939-7811-3_21.

Abstract

Soluble amyloid-β (Aβ) oligomers have become a focal point in the study of Alzheimer's disease due to their ability to elicit cytotoxicity. A number of recent studies have concentrated on the structural characterization of soluble Aβ oligomers to gain insight into their mechanism of toxicity. Consequently, providing reproducible protocols for the preparation of such oligomers is of utmost importance. The method presented in this chapter details a protocol for preparing an Aβ oligomer, with a primarily disordered secondary structure, without the need for chemical modification or amino acid substitution. Due to the stability of these disordered Aβ oligomers and the reproducibility with which they form, they are amenable for biophysical and high-resolution structural characterization.

Keywords: Alzheimer’s disease; Amyloid-β; NMR; Oligomer; Protein aggregation; Purification.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / isolation & purification*
  • Magnetic Resonance Spectroscopy
  • Protein Aggregates*
  • Protein Aggregation, Pathological
  • Protein Multimerization*
  • Protein Stability

Substances

  • Amyloid beta-Peptides
  • Protein Aggregates