Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Biochemistry. 2010 Feb 23;49(7):1358-60. doi: 10.1021/bi902005t.
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.
越来越多的证据将淀粉样β肽（Abeta）的原纤维前寡聚体与阿尔茨海默病的细胞毒性联系起来，可能是通过破坏生物膜。刚果红（CR）影响蛋白质聚集。已知它会自组装成胶束样组装体，但仍能降低细胞培养物和模式生物中 Abeta 聚集物的毒性。我们在这里表明，CR 以与阴离子去污剂相似的方式与 Abeta（1-40）相互作用。尽管 CR 促进β片层形成和肽聚集，但它也可能溶解毒性蛋白，使其对关键细胞成分的危害性降低，从而降低淀粉样毒性。
