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. 2020 Aug 25;37:101701. doi: 10.1016/j.redox.2020.101701

Fig. 2.

Fig. 2

OPC-B2 directly bindsto AKT and inhibits its activity. A.Cell viability of Huh7 cells after transfected with Myc-AKT1 and immunoblots of whole cell lysates from Huh7 cells. B.Cell viability of Huh7 cells treated with MK-2206 at a dose of 2 μM and immunoblots of whole cell lysates from Huh7 cells treated with MK-2206 for 24 h. C.Cell viability of Huh7 cells at different time points treated with OPC-B2 at doses of 50 and 75 μg/ml. D.Phosphorylation levelsof AKT at serine 473 (S473) and threonine 308 (T308) after treated with OPC-B2. E.Molecular docking indicates that OPC-B2 directly binds to the AKT1. F.Hydrogen bondsbetween AKT and OPC-B2. G.Detailed interaction residues of PH and kinase domain of AKT1 between OPC-B2 and AKT1. H.Immunoblots of purified activated GST-AKT1 protein incubated with OPC-B2 (75 μg/ml) for 15min and quantitative result of p-AKT(S473). I.A schematic model ofOPC-B2 binding to AKT1 directly. J.Immunoblots of cell lysates of Huh7 cells transfected with myc-AKT1, myc-AKT1(K297A) and myc-AKT1(R86A), followed by treatment with control solvent or OPC-B2 (75 μg/ml).The upper band is the exogenously overexpressed AKT1 protein, and the lower band is the endogenous AKT1 protein. K, L.Cell number of Huh7 cells transfected with myc-AKT1, myc-AKT1(R86A) and myc-AKT1(K297A), followed by treatment with control solvent or OPC-B2 (75 μg/ml) at different time points.Two-tailed Student's t-test,*p < 0.05; **p < 0.01; ***p < 0.001.