Open AccessBicine promotes rapid formation of β-sheet-rich amyloid-β fibrils
Author(s) -
Hye Yun Kim,
Hee Yang Lee,
Jong Kook Lee,
Hyunjin Vincent Kim,
Key Sun Kim,
Young Soo Kim
Publication year - 2020
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0240608
Subject(s) - cerebral amyloid angiopathy , in vitro , fibril , amyloid (mycology) , chemistry , biophysics , gene isoform , amyloid fibril , angiopathy , pathology , biochemistry , amyloid β , biology , medicine , dementia , endocrinology , disease , gene , diabetes mellitus
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, Aβ 40 is a valuable target in cerebral amyloid angiopathy research. However, the slow process of Aβ 40 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 Aβ 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 Aβ 40 with high speed and reproducibility, yielding a mixture of aggregates with significant β-sheet-rich fibril formation and toxicity.