Abstract
We have studied the binding interaction of N-ferrocenylmethyl-2-nitroaniline (2FMNA), N-ferrocenylmethyl-3-nitroaniline (3FMNA), and N-ferrocenylmethyl-4-nitroaniline (4FMNA) with bovine serum albumin (BSA) by absorption spectroscopy, cyclic voltammetry, and molecular docking techniques. The results indicated that these derivatives could bind to BSA and cause conformational changes in the order 3FMNA > 2FMNA > 4FMNA. Molecular docking study indicated the preferred binding site, binding mode and further suggested that the binding mode of the three compounds to BSA is of hydrogen bonding and hydrophobic forces, moreover the compound 2FMNA additionally shows a π-π stacking interaction.
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