Amyloids and Protein Aggregation—Analytical Methods
Peptides and Proteins
Published Online: 15 SEP 2009
Copyright © 2000 John Wiley & Sons, Ltd. All rights reserved.
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. .
- Published Online: 15 SEP 2009
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.
- X-ray diffraction;
- dye binding;