Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches

Asad Jan, Hilal A. Lashuel

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

Abstract

Aggregation and fibril formation of the amyloid-β (Aβ) peptides play a pivotal role in the pathogenesis of Alzheimer's disease (AD). The missing links on the pathway to Aβ oligomerization, fibril formation, and neurotoxicity in AD remain the identity of the toxic Aβ species and mechanism(s) of their toxicity. Such information is crucial for the development of mechanism-based therapeutics to treat AD and tools to diagnose and/or monitor the disease progression. Herein, we describe a simple approach that combines standard biophysical methods with cell biology assays to correlate the aggregation state of Aβ peptides with their cytotoxicity in vitro. The individual assays are well-established, commonly used, rely on easily accessible materials and can be performed within 24 h.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
Pages227-243
Number of pages17
Volume849
DOIs
Publication statusPublished - 1 Dec 2012
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume849
ISSN (Print)10643745

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Keywords

  • Alzheimer's disease
  • Amyloid-β
  • Oligomers
  • Toxicity

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Medicine(all)

Cite this

Jan, A., & Lashuel, H. A. (2012). Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches. In Methods in Molecular Biology (Vol. 849, pp. 227-243). (Methods in Molecular Biology; Vol. 849). https://doi.org/10.1007/978-1-61779-551-0_16