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P3‐065: POTENT INHIBITORS FOR OLIGOMERIC B‐AMYLOID AGGREGATION
Author(s) -
Wong Man Shing,
Yang Wanggui,
Xu Di,
Guo Lei,
Ho SeeLok,
Chan HoMan,
Li HungWing
Publication year - 2014
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2014.05.1153
Subject(s) - cyanine , chemistry , peptide , circular dichroism , amyloid (mycology) , amyloid disease , thioflavin , cytotoxicity , carbazole , fibril , biophysics , stereochemistry , fluorescence , biochemistry , in vitro , amyloid fibril , amyloid β , alzheimer's disease , organic chemistry , inorganic chemistry , disease , pathology , quantum mechanics , biology , medicine , physics
sonicated fibrils or cross-linked oligomers of Ab40, Ab42, and aS affected their aggregation pathways using thioflavin T(S) assay and electron microscopy.Results: Fibrils and oligomers of Ab40, Ab42, and aS acted as seeds, and affected the aggregation pathways within and among species. The seeding effects of aS fibrils were higher than those of Ab40 and Ab42 fibrils in the Ab40 and Ab42 aggregation pathways, respectively. Conclusions: We showed that Ab and aS acted as seeds and affected each other’s aggregation pathways in vitro, which may contribute to our understanding of the molecular mechanisms of interactions between AD and LBD pathologies.