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Amyloids and Protein Aggregation—Analytical Methods

Peptides and Proteins

  1. Huiyuan Li1,
  2. Farid Rahimi1,
  3. Sharmistha Sinha1,
  4. Panchanan Maiti1,
  5. Gal Bitan1,
  6. Kazuma Murakami2

Published Online: 15 SEP 2009

DOI: 10.1002/9780470027318.a9038

Encyclopedia of Analytical Chemistry

Encyclopedia of Analytical Chemistry

How to Cite

Li, H., Rahimi, F., Sinha, S., Maiti, P., Bitan, G. and Murakami, K. 2009. Amyloids and Protein Aggregation—Analytical Methods. Encyclopedia of Analytical Chemistry. .

Author Information

  1. 1

    University of California at Los Angeles, California, USA

  2. 2

    Metropolitan Institute of Gerontology, Tokyo, Japan

Publication History

  1. Published Online: 15 SEP 2009

Abstract

More than 30 diseases are associated with amyloid-forming proteins, which undergo conformational alterations and “misfolding” under particular conditions. These proteins deposit as insoluble proteinaceous aggregates generating disease-specific histopathologic lesions. The proteins contributing to each disease have dissimilar sequences and native structures, yet they share the commonality of forming insoluble amyloid aggregates characterized by fibrillar morphology and cross-β structure. Presently, it is thought that the predominant agents causing cell toxicity and tissue damage are soluble, prefibrillar assemblies of these proteins. Because of the metastable nature of these prefibrillar assemblies and the noncrystalline nature of fibrillar protein aggregates, structural study of amyloid proteins is difficult. As a result, structural characterization of these proteins is typically done using combinations of low-resolution analytical methods. Here, we present a compendium of analytical methods used to study the secondary, tertiary, and quaternary structures, and morphology of prefibrillar and fibrillar assemblies of amyloid-forming proteins.

Keywords:

  • amyloid;
  • fibril;
  • oligomer;
  • microscopy;
  • NMR;
  • X-ray diffraction;
  • dye binding;
  • spectroscopy;
  • chromatography;
  • cross-linking;
  • electrophoresis