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Bicine promotes rapid formation of ?-sheet-rich amyloid-? fibrils.

ABSTRACT: Fibrillar aggregates of amyloid-? (A?) are the main component of plaques lining the cerebrovasculature in cerebral amyloid angiopathy. As the predominant A? isoform in vascular deposits, A?40 is a valuable target in cerebral amyloid angiopathy research. However, the slow process of A?40 aggregation in vitro is a bottleneck in the search for A?-targeting molecules. In this study, we sought a method to accelerate the aggregation of A?40 in vitro, to improve experimental screening procedures. We evaluated the aggregating ability of bicine, a biological buffer, using various in vitro methods. Our data suggest that bicine promotes the aggregation of A?40 with high speed and reproducibility, yielding a mixture of aggregates with significant ?-sheet-rich fibril formation and toxicity.

SUBMITTER: Kim HY

PROVIDER: S-EPMC7553346 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Bicine promotes rapid formation of β-sheet-rich amyloid-β fibrils.

Kim Hye Yun HY Lee HeeYang H Lee Jong Kook JK Kim Hyunjin Vincent HV Kim Key-Sun KS Kim YoungSoo Y

PloS one 20201013 10

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 vascular deposits, Aβ40 is a valuable target in cerebral amyloid angiopathy research. However, the slow 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, to improve experimental screening procedures. We ev ...[more]

PMID: 33048999

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