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Simultaneous Monitoring of Amyloid-ß (Aß) Oligomers and Fibrils for Effectively Evaluating the Dynamic Process of Aß Aggregation.

ACS Sens; 4(2): 471-478, 2019 Feb 22.
Artigo em Inglês | MEDLINE | ID: mdl-30693761
Herein, we provide a proof of concept for a novel strategy that targets the assessment of the aggregation of amyloid-ß (Aß) by simultaneously determining its oligomers (Aßo) and fibrils (Aßf) in one analytical system. By fabricating and combining two immunosensors for Aßo and Aßf, respectively, we constructed a two-channel electrochemical system. The ratio of Aßf to Aßo was calculated and taken as a possible criterion for evaluating the extent of aggregation. Thereby, the presence of and transformation between oligomers and fibrils were accurately probed by incubating the Aß monomer for different times and then calculating the ratios of Aßf to Aßo. The applicability of this method was further validated by tracking the dynamic progress of Aß aggregation in the cerebrospinal fluid and tissues of Alzheimer's disease (AD) rats, which revealed that the ratio of Aßf to Aßo in rat brain gradually increased with the progression of AD, which was indicative of the severity of peptide aggregation during this process. Overall, this study represents the first example of a quantitative strategy for precisely evaluating the aggregation process that is related to pathological events in AD brain.