RESUMO
ß-amyloid hypothesis is the predominant hypothesis in the study of pathogenesis of Alzheimer's disease. This hypothesis claims that aggregation and neurotoxic effects of amyloid ß (Aß) is the common pathway in a variety of etiological factors for Alzheimer's disease. Aß peptide derives from amyloid precursor protein (APP). ß-sheet breaker peptides can directly prevent and reverse protein misfolding and aggregation in conformational disorders. Based on the stereochemical structure of Aß1-42 and aggregation character, we had designed a series of ß-sheet breaker peptides in our previous work and screened out a 10-residue peptide ß-sheet breaker peptide, H102. We evaluated the effects of H102 on expression of P-tau, several associated proteins, inflammatory factors and apoptosis factors, and examined the cognitive ability of APP transgenic mice by behavioral test. This study aims to validate the ß-amyloid hypothesis and provide an experimental evidence for the feasibility of H102 treatment for Alzheimer's disease.
