Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches. Academic Article uri icon

Overview

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.

publication date

  • January 1, 2012

Research

keywords

  • Amyloid beta-Peptides
  • Biological Assay
  • Biophysical Phenomena
  • Peptide Fragments
  • Protein Multimerization

Identity

Scopus Document Identifier

  • 84864619211

Digital Object Identifier (DOI)

  • 10.1007/978-1-61779-551-0_16

PubMed ID

  • 22528094

Additional Document Info

volume

  • 849