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. 2021 Apr 27;12:643188. doi: 10.3389/fphar.2021.643188

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Copyright © 2021 Lin, Zhang, Fan, Hou, Wang, Zhu, Tian, An and Yan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Molecular docking of Frutescone O on TLR4-MD2 complex. (A) The close-up view and 2D view of the sites of Fru in the TLR4-MD2 complex. (B) The close-up view and 2D view of the sites of TAK242 in the TLR4-MD2 complex. (C) The close-up view and 2D view of the sites of Sparstolonin B in the TLR4-MD2 complex. (D) The close-up view and 2D view of the sites of Procyanidin B1 in the TLR4-MD2 complex. (E, F) The binding study of TLR4 with Fru (0.8 μM) by cellular thermal shift assay. Rb1 (40 μM) served as the positive control and 0 the negative control. Quantitative data was represented as mean ± SD (n = 3, *p < 0.05, **p < 0.01, ***p < 0.001 vs. negative control).