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A variety of biological activities, such as anti-microbial and anti-tumor properties was reported for 1,10-phenanthroline and its copper complexes. In this study, the anti-proliferative activity of a novel  [Cu(L)(phen)] complex was investigated on MCF-7 breast cancer cells using MTT assay. Since chemotherapy is lake of ability to distinguish between normal cells from cancerous cells, therefore we also investigated the effect of  [Cu(L)(phen)] complex on normal L929 cells. The results showed that following 24 and 48 h exposure of cells with  [Cu(L)(phen)] complex, the IC50 values for MCF-7 were significantly lower than that recorded for L929 and normal cells were less sensitive than cancerous cells to the complex. Additionally, the  [Cu(L)(phen)] complex displayed a time- and concentration-dependent cytotoxic response, with MCF-7 and L929 cells. Also flow cytometry findings suggest that  [Cu(L)(phen)] complex is capable of decreasing cancer cell viability through apoptosis and did not efficiently activate the necrosis process.

Recent advances have put fundamental focus on the application of copper (II) (Cu [II]) complexes as agents for fighting against cancer. To determine whether [Cu(L)(2imi)] complex as a novel Cu complex can induce apoptosis in HepG2 as cancerous cells and L929 as normal cells via extrinsic or intrinsic apoptotic pathways, both cell lines were treated for 24 and 48 hours at IC 50 concentrations of [Cu(L)(2imi)] complex. Then, the expression of some apoptosis-related genes including p53, caspase-8, bcl-2, and bax were assayed by real-time polymerase chain reaction. The [Cu(L)(2imi)] complex seems to inhibit the expression of bcl-2 in complex-treated HepG2 cancerous cells following the 24-and 48-hour treatment. The complex upregulated the p53, bax, and caspase-8 genes, therefore treatment of HepG2 cancerous cells with [Cu(L)(2imi)] complex induces programmed cell death via the upregulation of relative bax/bcl-2 ratio. Finally, this copper complex triggered apoptosis in HepG2 cells via both intrinsic and extrinsic pathway, whereas treatment of normal L929 cells with this complex induce apoptosis only via intrinsic pathway with the upregulation of relative bax/bcl-2 ratio and does not affect the expression level of caspase-8 gene and does not trigger the extrinsic pathway. Finally, these results obtained from present study confirm the role of a novel Cu complex on the induction of apoptosis process in HepG2 and L929 cells by overexpression of bax, inhibition of bcl-2 and increase of the relative bax/bcl-2 ratio. These results support that the [Cu(L)(2imi)] complex is able to induce apoptosis in cancerous cells, therefore, it has a potential for development as a novel anticancer drug. K E Y W O R D S bax, bcl-2, caspase-8, [Cu(L)(2imi)] complex, hepatocellular carcinoma, p53

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The study aimed at investigating the binding features of the mixed ligand Copper (II) complex to BSA and DNA. Both in‐silico and in‐vitro analyses were made to fully assess the binding mechanism and mode of the Copper (II) complex to BSA and DNA. Spectroscopic tests demonstrated the Copper (II) complex reacted with DNA through binding to its minor grooves with the association constant 3.36×103 M−1. This type of interaction was confirmed by molecular docking simulations. Tryptophan quenching analyses at 298, 303 and 308 K showed that the Copper (II) complex reacted with the BSA's ground‐state fluorophore and created a non‐fluorescent adduct. In other words, a static quenching approach was offered with the quenching rate constants within the span of 3.4×1012‐1.28×1013 M−1s−1. Besides, the values of binding constants at various temperatures were achieved, implying the moderate similarity of the Copper (II) complex to the serum's albumin. Research on thermodynamic factors suggested the complex‐BSA bond was an enthalpy‐induced reaction where Van der Waals forces and the hydrogen bond performed the leading role. The simulations of molecular docking verified the test results and demonstrated the amino acids engaged in the bond between BSA and the Copper (II) complex.