Investigation on the Effect of Fluorescence Quenching of Calf Thymus DNA by Piperine: Caspase Activation in the Human Breast Cancer Cell Line Studies

, respectively, which suggested the dominance of dynamic mechanism as the fluorescence quenching of piperine-ctDNA. The thermodynamic parameters revealed the predominance of hydrophobic forces in the interaction of ctDNA with piperine. According to the resonance light scattering data, the formation of a complex between piperine and ctDNA led to the creation of a larger particle. Ethidium bromide (EB) and acridine orange (AO) displacement studies, along with the ionic effects of NaCl and KI assessments, confirmed the interaction of piperine-ctDNA through a groove binding mode. The melting temperature assay of ctDNA upon the addition of piperine concentration indicated the probable groove binding of piperine to ctDNA, which was affirmed by relative viscosity measurement as well. The lack of detecting any alterations in the circular dichroism (CD) spectrum of CD investigation verified as a characteristic sign of groove binding mechanism and also confirmed all the experimental results with regard to the binding of piperine-ctDNA complex. Next to observing a concentration and time-dependent cytotoxicity in MDA-MB-231 cells, the impact of piperine on increasing lipid peroxidation and decreasing the activity of superoxide dismutase was also noticed. Apparently, piperine is capable of inducing caspase-3 activity as well.