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Start Over Author "Wahlström, Anna" Journal biochemistry
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3. Detergent-like interaction of Congo red with the amyloid beta peptide.

Author

Lendel C, Bolognesi B, Wahlström A, Dobson CM, and Gräslund A

Subjects
Amyloid beta-Peptides antagonists & inhibitors, Amyloid beta-Peptides toxicity, Amyloid beta-Peptides ultrastructure, Anions chemistry, Anions metabolism, Magnetic Resonance Spectroscopy, Microscopy, Electron, Transmission, Peptide Fragments antagonists & inhibitors, Peptide Fragments toxicity, Peptide Fragments ultrastructure, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Secondary, Amyloid beta-Peptides metabolism, Congo Red chemistry, Congo Red metabolism, Detergents chemistry, Detergents metabolism, Peptide Fragments metabolism
Abstract

Accumulating evidence links prefibrillar oligomeric species of the amyloid beta peptide (Abeta) to cellular toxicity in Alzheimer's disease, potentially via disruption of biological membranes. Congo red (CR) affects protein aggregation. It is known to self-associate into micelle-like assemblies but still reduces the toxicity of Abeta aggregates in cell cultures and model organisms. We show here that CR interacts with Abeta(1-40) in a manner similar to that of anionic detergents. Although CR promotes beta sheet formation and peptide aggregation, it may also solubilize toxic protein species, making them less harmful to critical cellular components and thereby reducing amyloid toxicity.

Published
2010
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