Detergent-like interaction of Congo red with the amyloid beta peptide.
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.
Lendel
Christofer
C
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. lendel@kth.se
Bolognesi
Benedetta
B
Wahlström
Anna
A
Dobson
Christopher M
CM
Gräslund
Astrid
A
D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors / Q000378:metabolism* / Q000633:toxicity / Q000648:ultrastructure; D000838:Anions / Q000737:chemistry / Q000378:metabolism; D003224:Congo Red / Q000737:chemistry* / Q000378:metabolism*; D003902:Detergents / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D046529:Microscopy, Electron, Transmission; D010446:Peptide Fragments / Q000037:antagonists & inhibitors / Q000378:metabolism* / Q000633:toxicity / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides; D000838:Anions; D003902:Detergents; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D003224:Congo Red