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Cytotoxicity and antioxidant activity of Kamolonol acetate from Ferula pseudalliacea, and studying its interactions with calf thymus DNA (ct-DNA) and human serum albumin (HSA) by spectroscopic and molecular docking techniques

Hanie Mahaki, Hamid Tanzadehpanah, Osama K. Abou-Zied, Neda Hosseinpour Moghadam, Asrin Bahmani, Sadegh Salehzadeh, Dara Dastan, Massoud Saidijam
Process biochemistry 2019 v.79 pp. 203-213
2,2-diphenyl-1-picrylhydrazyl, DNA, Ferula, acetates, antioxidant activity, binding properties, binding sites, bioactive compounds, calves, cell lines, colorectal neoplasms, computer simulation, cytotoxicity, electrostatic interactions, fluorescence, human serum albumin, hydrophobic bonding, inhibitory concentration 50, median effective concentration, mesenchymal stromal cells, neoplasm cells, spectroscopy, thymus gland, viscosity, zeta potential
In this study, kamolonol acetate (KamA) was extracted from Ferula pseudalliacea and its cytotoxicity, antioxidant activities, calf thymus DNA (DNA) and human serum albumin (HSA) binding properties were evaluated by several methods. The cytotoxicity of the KamA against two colorectal cancer cell lines (HCT116 and CT26) and two normal cell lines (mesenchymal stem cells and Vero cells) was determined with IC50 values of 27, 17, 47, and 72 μM, respectively. KamA also showed a potent antioxidant activity on the DPPH radical scavenging (EC50 = 65.29 μM). The results obtained from DNA binding evaluations using DNA competitive displacement and viscosity measurements showed that KamA can bind to DNA via an intercalation mode. Binding activity of HSA exhibited that KamA can strongly quench the intrinsic fluorescence of HSA through a static quenching mode (distance = 2.22 nm). We also found that the KamA binding site on HSA is located in sub-domain IIA. Furthermore, the zeta-potential measurements showed that both electrostatic and hydrophobic interactions play a critical role in the formation of [DNA-KamA] and [HSA-KamA] complexes. Finally, molecular docking supported the experimental results in binding sites and binding forces. As a conclusion, we suggested that KamA can be introduced as a bioactive compound.