Kim, Hye Yun Lee, HeeYang Lee, Jong Kook Kim, Hyunjin Vincent Kim, Key-Sun Kim, YoungSoo 2024-01-19T16:32:48Z 2024-01-19T16:32:48Z 2021-09-02 2020-10 1932-6203 https://pubs.kist.re.kr/handle/201004/118083 Fibrillar aggregates of amyloid-beta (A beta) are the main component of plaques lining the cerebrovasculature in cerebral amyloid angiopathy. As the predominant A beta isoform in vascular deposits, A beta(40) is a valuable target in cerebral amyloid angiopathy research. However, the slow process of A beta(40) aggregationin vitrois a bottleneck in the search for A beta-targeting molecules. In this study, we sought a method to accelerate the aggregation of A beta(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 beta(40) with high speed and reproducibility, yielding a mixture of aggregates with significant beta-sheet-rich fibril formation and toxicity. English PUBLIC LIBRARY SCIENCE Bicine promotes rapid formation of beta-sheet-rich amyloid-beta fibrils Article 10.1371/journal.pone.0240608 1 PLOS ONE, v.15, no.10 PLOS ONE 15 10 N scie scopus 000581813300042 2-s2.0-85092885623 Multidisciplinary Sciences Science & Technology - Other Topics Article ALZHEIMERS-DISEASE PEPTIDE A-BETA(1-40) ANGIOPATHY FIBRILLOGENESIS AGGREGATION BUFFERS