Decoding the binding interaction of steroidal pyridines with bovine serum albumin using spectroscopic and molecular docking techniques

The present study reports a comprehensive and conformational aspect of binding of steroidal pyridines (1-6) with a model transport protein, bovine serum albumin (BSA) by fluorescence, UV-visible, circular dichroism, and molecular docking techniques. Quenching of BSA emission was attributed to the formation of the ground state complex after the compound (1-6) binds to the backbone of the protein. Synchronous fluorescence spectra re-veals changes in the microenvironment of the aromatic residues. UV-visible absorption spectra further reiterate the quenching mechanism to be static and binding of compound (1-6) results in the formation of a ground-state complex. Circular dichroism spectra indicated that compound 1-3 causes unfolding and compound 4-6 leads to the stabilization of the protein structure. In addition, a molecular docking study revealed the binding pocket for the formation of the ligand-protein complex through hydrogen bonding and hydrophobic interactions. Furthermore, hemolytic activity suggested that the compounds (1-6) are biocompatible in nature. Evaluation of such steroid-protein interaction helps in better understanding of the biomolecular interaction of steroidal compounds with biomacromolecule and opens up new approaches in steroid based drug-design process.