A water-soluble cationic gallium corrole, 5,10,15-tris(N-methyl-4-pyridyl)corrolatogallium(III) (3), was prepared and characterized. The photocytotoxicity of 3 was investigated using Hep G2 cancer cell line. Upon treatment with corrole 3 and irradiation, fragmentation of tumor cell nuclei was observed, which led to apoptosis. Flow cytometric analysis clearly showed the efficient induction of apoptotic cell death, and corrole 3 exhibited high photocytotoxicity towards Hep G2 cancer cells (IC 50 = 60 nM). Furthermore, the binding behavior of corrole 3 with c-MYC G-quadruplex DNA, a potent target for antitumor drugs, was investigated using spectroscopic methods and molecular docking simulation.

The DNA binding of amphiphilic iron(III) 2,17-bis(sulfonato)-5,10,15-tris(pentafluorophenyl)corrole complex (Fe-SC) was studied using spectroscopic methods and viscosity measurements. Its nuclease-like activity was examined by using pBR322 DNA as a target. The interaction of Fe-SC with human serum albumin (HSA) in vitro was also examined using multispectroscopic techniques. Experimental results revealed that Fe-SC binds to ct-DNA via an outside binding mode with a binding constant of 1.25 × 10(4) M(-1). This iron corrole also displays good activity during oxidative DNA cleavage by hydrogen peroxide or tert-butyl hydroperoxide oxidants, and high-valent (oxo)iron(V,VI) corrole intermediates may play an important role in DNA cleavage. Fe-SC exhibits much stronger binding affinity to site II than site I of HSA, indicating a selective binding tendency to HSA site II. The HSA conformational change induced by Fe-SC was confirmed by UV/Vis and CD spectroscopy.

The first oxidative cleavage of DNA by manganese N-confused porphyrin [chloro(2aza-2-methyl-5,10,15,20-tetrakis(p-chlorophenyl)-21-carbaporphyrin)manganese(III), 1] using H 2 O 2 as oxidant agent and its magnetic, calf thymus DNA(ct-DNA)-and human serum albumin (HSA) binding properties were investigated. The magnitude of the axial (D) zero-field splitting for the mononuclear Mn(III) center in 1 was determined to be approximately 2.71 cm -1 by paramagnetic susceptibility measurements. The DNA-and HSA binding experimental results showed that 1 bound to ct-DNA via an outside groove binding mode and the hydrophobic cavity located in subdomain IIA of HSA with the binding constant of 4.144 × 10 5 M -1 and ~10 6 M -1 , respectively. Thermodynamic parameters revealed that both DNA-and HSA binding were spontaneous process. The main driven forces were the hydrogen bond and van der Waals for the former, but hydrophobic interaction for the latter, which were further confirmed by molecular docking modeling. Manganese N-confused porphyrin 1 could cleave the supercoiled plasmid DNA efficiently in the presence of hydrogen peroxide. Hydroxyl radical ( · OH) was found the active species for oxidative damage of DNA.