Alzheimer's and prion disease as disorders of protein conformation: implications for the design of novel therapeutic approaches.
Several lines of evidence suggest that a defective protein folding is a central event in both Alzheimer's and prion disease. Although the two disorders are very different clinically, neuropathologically, and biochemically, the molecular event that may trigger the disease process appears to be the same: the formation of an altered protein conformer composed of a high content of beta-sheet structure. Compounds with the ability to prevent and to reverse protein conformational changes may be useful as novel therapeutic approaches for Alzheimer's disease, prion disease, and other disorders of defective protein folding.
Soto
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Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago. sotojc01@popmail.med.nyu.edu
D000544:Alzheimer Disease / Q000188:drug therapy* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics; D001923:Brain Chemistry; D006801:Humans; D009154:Mutation; D010455:Peptides / Q000627:therapeutic use*; D017096:Prion Diseases / Q000188:drug therapy* / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides; D010455:Peptides; D011328:Prions