Improvement of Load Bearing Capacity of Nanoscale Superlow Friction by Synthesized Fluorinated Surfactant Micelles

Although surfactant micelles usually exhibit superlow friction at the nanoscale due to the formation of the hydration layer, the load-bearing capacity (LBC) is limited. In this study, the friction behaviors of two different surfactant micelles (fluorinated and hydrocarbon surfactants, denoted as F-surfactant and H-surfactant) were compared, with the results showing that both can achieve superlow friction (μ = 0.001–0.002) when the self-assembled micelle layers on the two surfaces were not ruptured. Although the two different surfactant micelles have the similar friction behaviors, the LBC of superlow friction for the F-surfactant is 2.5 times larger than that for the H-surfactant. The mechanisms of the superlow friction and the reasons for different LBC were investigated using an atomic force microscopy. The superlow friction can be attributed to the formation of hydration layer on the surfactant headgroups, whereas the higher LBC for F-surfactant originates from the fatness of its carbon chain, which produces the larger hydrophobic attraction and meanwhile increases the stiffness of the micelle layer

Jolkinolide B downregulates the protein of MSI2 and the p53 expression in HCC cells.

(A, C) Huh-7 and (B, D) SK-Hep-1 cells were treated with the indicated concentrations of Jolkinolide B for 48 h. The MSI2 and p53 protein expressions were analyzed using western blotting. GAPDH was used as an internal control. *p p p <0.001.</p

Jolkinolide B inhibits HCC cell lines migration, invasion and promotes HCC cell apoptosis.

(A) Huh-7 and SK-Hep-1 cells were seeded, scratched, and then treated with Jolkinolide B at a concentration of 10 μM for 48 h. The wound healing assays were performed to assess the migration abilities of Huh-7 and SK-Hep-1 cells. (B) Huh-7 and SK-Hep-1 cells were seeded in the upper transwell chamber and treated with DMSO or Jolkinolide B of 10 μM for 48 h to evaluate the migration and invasion abilities of HCC cells. (C) Huh-7 and SK-Hep-1 cells were treated with DMSO or Jolkinolide B at a concentration of 10 μM for 48 h; then the protein expression of E-cadherin and vimentin was analyzed using western blotting. GAPDH was used as an internal control. (D) Western blotting was used to assess Bax and BCL-2 protein expressions. GAPDH was used as an internal control. The relative protein intensities were analyzed. (E) Huh-7 and SK-Hep-1 cells were treated with DMSO or Jolkinolide B, the cells apoptosis was analyzed by flow cytometry and apoptosis rates were calculated. *p p p <0.001.</p

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Slide 1: Original images for Fig 2A, 2B, 2E. Slide 2: Original immunoblots for Fig 2C, 2D. Slide 3: Original immunoblots for Fig 3. Slide 4: Original immunoblots for Fig 4. Slide 5: Original immunoblots for Fig 5A, 5C. Slide 6: Original immunoblots for Fig 6A, 6B. Slide 7: Original immunoblots for Fig 6C. Sheet 1: Original CCK8 of cell viability for Fig 1A-1C. Original RT-qPCR for Figs 3C, 3D, 5B. (ZIP)</p

Jolkinolide B inhibits HCC cells proliferation.

Cell viability assays of Huh-7 (A), SK-Hep-1 (B) and L-02 cells (C) were performed using CCK-8 method after treatment with different concentrations (0, 5, 10, 25, 50, or 100 μM) of Jolkinolide B for 48 h.</p

Overexpression of MSI2 reverses Jolkinolide B-promoted apoptosis and Jolkinolide B-inhibited EMT and β-catenin signaling in HCC cells.

Huh-7 and SK-Hep-1 cells were treated with DMSO, 10 μM Jolkinolide B, or Jolkinolide B together with MSI2 plasmids. Then, the protein expressions of (A) Bax, BCL-2, (B) E-cadherin, vimentin and (C) β-catenin were analyzed using western blotting. GAPDH was used as an internal control. The relative protein intensities were analyzed. (D) Proposed working model of Jolkinolide B-induced inhibition of HCC. *p p p <0.001.</p