Bicine promotes rapid formation of β-sheetrich amyloid-β fibrils

Title
Bicine promotes rapid formation of β-sheetrich amyloid-β fibrils
Authors
김기선Hye Yun KimHeeYang LeeJong Kook LeeHyunjin Vincent KimYoungSoo Kim
Issue Date
2020-10
Publisher
PLoS ONE
Citation
VOL 15, NO 10-8
Abstract
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.
URI
http://pubs.kist.re.kr/handle/201004/71973
ISSN
1932-6203
Appears in Collections:
KIST Publication > Article
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