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Detergent-like interaction of Congo red with the amyloid beta peptide.
- Source :
-
Biochemistry [Biochemistry] 2010 Feb 23; Vol. 49 (7), pp. 1358-60. - Publication Year :
- 2010
-
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.
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 49
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 20070125
- Full Text :
- https://doi.org/10.1021/bi902005t