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

Hye Yun Kim, Hee Yang Lee, Jong Kook Lee, Hyunjin Vincent Kim, Key Sun Kim, Young Soo Kim

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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 evaluated the aggregating ability of bicine, a biological buffer, using various in vitro methods. Our data suggest that bicine promotes the aggregation of Aβ40 with high speed and reproducibility, yielding a mixture of aggregates with significant β-sheet-rich fibril formation and toxicity.

Original languageEnglish
Article numbere0240608
JournalPloS one
Issue number10 OCTOBER
Publication statusPublished - 2020 Oct

Bibliographical note

Funding Information:
This work was supported by National Research Foundation of Korea (NRF-2018R1A6A1A03023718 and NRF- 2018R1D1A1B07048857), and POSCO Science Fellowship of POSCO TJ Park Foundation. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

Publisher Copyright:
© 2020 Kim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

All Science Journal Classification (ASJC) codes

  • General


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