Analyzing Morphological Properties of Early-Stage Toxic Amyloid β Oligomers by Atomic Force Microscopy

Dusan Mrdenovic; Jacek Lipkowski; Piotr Pieta

doi:10.1007/978-1-0716-1843-1_18

Analyzing Morphological Properties of Early-Stage Toxic Amyloid β Oligomers by Atomic Force Microscopy

Methods Mol Biol. 2022:2402:227-241. doi: 10.1007/978-1-0716-1843-1_18.

Authors

Dusan Mrdenovic^{1

2}, Jacek Lipkowski², Piotr Pieta³

Affiliations

¹ Institute of Physical Chemistry, Polish Academy of Sciences, Warsaw, Poland.
² Department of Chemistry, University of Guelph, Guelph, ON, Canada.
³ Institute of Physical Chemistry, Polish Academy of Sciences, Warsaw, Poland. ppieta@ichf.edu.pl.

PMID: 34854048
DOI: 10.1007/978-1-0716-1843-1_18

Abstract

Protein misfolding diseases, like Alzheimer's, Parkinson's, and Huntington's disease, are associated with misfolded protein aggregation. Alzheimer's disease is related to a progressive neuronal death induced by small amyloid β oligomers. Here, we describe the procedure to prepare and identify different types of small toxic amyloid β oligomers by atomic force microscopy (AFM).

Keywords: Aggregation; Amyloid β; Aβ preparation; Oligomers; Protein misfolding.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alzheimer Disease
Amyloid
Amyloid beta-Peptides / toxicity
Humans
Microscopy, Atomic Force*

Substances

Amyloid
Amyloid beta-Peptides