Bicine promotes rapid formation of β-sheetrich amyloid-β fibrils
- Bicine promotes rapid formation of β-sheetrich amyloid-β fibrils
- 김기선; Hye Yun Kim; HeeYang Lee; Jong Kook Lee; Hyunjin Vincent Kim; YoungSoo Kim
- Issue Date
- PLoS ONE
- VOL 15, NO 10-8
- Fibrillar aggregates of amyloid-β (Aβ) are the main component of plaques lining the cerebrovasculature in cerebral amyloid angiopathy. As the predominant Aβ isoform in vasculardeposits, Aβ40 is a valuable target in cerebral amyloid angiopathy research. However, theslow process of Aβ40 aggregation in vitro is a bottleneck in the search for Aβ-targeting molecules. In this study, we sought a method to accelerate the aggregation of Aβ40 in vitro, toimprove experimental screening procedures. We evaluated the aggregating ability of bicine,a biological buffer, using various in vitro methods. Our data suggest that bicine promotes theaggregation of Aβ40 with high speed and reproducibility, yielding a mixture of aggregateswith significant β-sheet-rich fibril formation and toxicity.
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