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. 2018 May 23;9:532. doi: 10.3389/fphar.2018.00532

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Copyright © 2018 Wang, Tian, Zhang, Xu, Zhou, Wang, Lu, Luo, Wang, Sun, Xu and Sun.

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 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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Hsp90ab1 as potential target of CE-P. (A) The predicted proteins by Discovery Studio 2016 software. (B) Identified peptide of Hsp90ab1 by LC/MS (C) Western-blotting validation of the CE-P target Hsp90ab1 by whole cell lysate pull-down assay. (D) The pull-down assay of the recombinant Hsp90AB1 by CE-P. (E) CE-P could pull down Hsp90AB1 in dose-dependent manner. (F) CE could inhibit the binding to Hsp90AB1 and then the proteins bound to CE-P were detected by Western blot. (G) Effects of CE on Hsp90AB1 expression levels in ox-LDL induced HUVEC damage. Cell lysates were harvested, and Western blot analysis was performed. β-actin expression was examined as the protein loading control. (H) Densitometric analysis was used to quantify the levels of Hsp90AB1. Values are expressed as the mean ± SD ^#p < 0.05 ox-LDL group vs. control group; *p < 0.05, vs. ox-LDL group.