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Desentrañando los misterios del mal de Alzheimer: una enfermedad relacionada a alteraciones en la conformación de proteínas

© Claudio Soto, 1999


Alzheimer's disease is the most common cause of dementia in late-life. A hallmark event in this disease is the formation and deposition of protein aggregates named amyloid in the brain of people affect by this disorder. In this paper, I describe our recent efforts to understand the molecular basis of amyloid formation and the use of this knowledge for the design of a novel therapeutic approach. Our results suggest that the critical step in amyloid deposition is the conformational change of a 40-residue peptide, which is neurotoxic when adopting a pathological structure. To prevent and revert this conformational change, we have designed small peptides called anti-ß-sheet peptides, which inhibit amyloid formation and dissolve preformed fibrils in the test tube and in animal model brains. Furthermore, these peptides prevent cell death induced by amyloid in human neuronal culture assays. Our findings open a promising way for the generation of a treatment aimed at stopping the progression of neurodegeneration in Alzheimer's disease.