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    Acylphloroglucinols with acetylcholinesterase inhibitory effects from the fruits of Eucalyptus robusta

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    The accepted manuscript version of this article is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) License.
    Date Issued
    2020-10
    Publisher Version
    10.1016/j.bioorg.2020.104127
    Author(s)
    Liu, Hui
    He, Xiao-Zhi
    Feng, Mi-Yan
    Zeng, Yuan
    Rauwolf, Tyler J.
    Shao, Li-Dong
    Ni, Wei
    Yan, Hui
    Porco, John A.
    Hao, Xiao-Jiang
    Qin, Xu-Jie
    Liu, Hai-Yang
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    Permanent Link
    https://hdl.handle.net/2144/41448
    Version
    Accepted manuscript
    Citation (published version)
    Hui Liu, Xiao-Zhi He, Mi-Yan Feng, Yuan Zeng, Tyler J Rauwolf, Li-Dong Shao, Wei Ni, Hui Yan, John A Porco, Xiao-Jiang Hao, Xu-Jie Qin, Hai-Yang Liu. 2020. "Acylphloroglucinols with acetylcholinesterase inhibitory effects from the fruits of Eucalyptus robusta.." Bioorg Chem, Volume 103, pp. 104127 - ?. https://doi.org/10.1016/j.bioorg.2020.104127
    Abstract
    Eleven new acylphloroglucinols, including six new formylated phloroglucinol-monoterpene meroterpenoids, eucalyprobusals A-F (1-6), one monomeric acylphloroglucinol, eucalyprobusone B (7), and four dimeric acylphloroglucinols, eucalyprobusones C-F (8-11) were purified from the fruits of Eucalyptus robusta. The establishment of the structures of 1-11 was achieved by a combination of NMR and HRESIMS data analyses, electron circular dichroism (ECD), and single-crystal X-ray diffraction. Compounds 6, 8, and an inseparable mixture of 10 and 11 were found to be potent AChE inhibitors with IC50 values of 3.22 ± 0.36, 3.82 ± 0.22, and 2.55 ± 0.28 μΜ, respectively. Possible interaction sites of 6, 8, 10, and 11 with AChE were investigated by means of molecular docking studies, and the results revealed that AChE residues Asn87, Ser125, Thr83, Tyr133, Tyr124, Tyr337, and Tyr341 played crucial roles in the observed activity of the aforementioned compounds.
    Rights
    The accepted manuscript version of this article is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) License.
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    • CAS: Chemistry: Scholarly Papers [127]
    • BU Open Access Articles [3866]


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