The aims of this study were to characterize the curcumin/cyclodextrin polymer inclusion complex using X-ray diffractometry (XRD), Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and UV–vis spectroscopy, and to determine the antioxidant activity of this complex by methods of scavenging 2,2-azinobis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radicals assays and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals assays. The inhibitory effect of inclusion complex on A375 cells was also investigated by CCK-8 assay, Annexin-V/PI staining assay, and caspase activity assay. The results showed that the complex exhibited different physicochemical characteristics from that of free curcumin. Moreover, the inclusion complex exhibited novel antioxidant activity by scavenging the ABTS and DPPH free radicals and displayed higher antiproliferative activity on A375 cells. Further investigation revealed that inclusion complex could induce A375 cell apoptosis. These findings suggest that inclusion complex could be developed as a novel natural antioxidant with potential applications in cancer chemoprevention.

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Background Tubeimoside I (TBMS1) was isolated from the tubers of Bolbostemma paniculatum (Maxim.) Franquet. TBMS1 shows potent anti-tumor activity. The present study was conducted to investigate the anti-microtubule role of TBMS1 and its binding site of tubulin. Methods Cell growth inhibition was measured by MTT after treatment with TBMS1. Uptake kinetics of TBMS1 by human nasopharyngeal carcinoma CNE-2Z cell line (CNE-2Z) was assayed by HPLC. Microtubule protein (MTP) was prepared from porcine brain through two cycles of polymerization-depolymerization in a high molarity buffer. Inhibition of MTP polymerization induced by TBMS1 was determined by a turbidity measurement and a sedimentation assay; the interactions of TBMS1 with tubulin within CNE-2Z cells were investigated by immunofluorescence microscopy and immunoblotting. TBMS1 was tested for its ability to inhibit binding of known tubulin ligands through competitive binding assay. Results TBMS1 displayed growth inhibitory activity against CNE-2Z cells with IC 50 value of 16.7 lM for 72 h. HPLC analysis of TBMS1 uptake by CNE-2Z cells displayed the initial slow TBMS1 uptake and then gradually reaching an maximum uptake near 18 h. CNE-2Z cells treated with TBMS1 (25 lM, 3 h) were sufficient to cause the microtubular network disruption. Immunoblot analysis showed that the proportion of cytosolic tubulin of cells treated with TBMS1 increased in a time-and concentration-dependent manner. TBMS1 did not inhibit the binding of vinblastine to tubulin. Colchicine binding to tubulin was inhibited in the presence of TBMS1. Conclusions TBMS1 is an anti-microtubule agent, and its binding site of tubulin is the colchicine binding site of tubulin.

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