Modulation of the Protein-Ligand Interaction in the Presence of Graphene Oxide: a Detailed Spectroscopic Study

Several applications of graphene oxide (GO) have been established over the years, and it has the potential to be used as a biomedical material. Studying the effect of GO on protein-ligand (small molecules/drugs) complex systems are vital as the mechanisms involved are not well understood. The interaction of GO on the protein-ligand binding is also vital for the preparation of an effective drug carrier in the bloodstream. In this work, we have tried to explore in details the effect of GO on the interaction between a hydrophilic molecule, namely, 7-(N,N'-diethylamino) coumarin-3-carboxylic acid (7-DCA) with human serum albumin (HSA) by employing multispectroscopic, microscopic, calorimetric, and molecular docking studies. We find out that protein-ligand complexes were placed on the GO surface, and GO gives stability to the protein-ligand complex via hydrogen bonding, electrostatic interactions, hydrophobic interactions, and so forth. Due to the presence of a large surface area in GO, it offers a hydrophobic environment, and as a result, the emission maxima of 7-DCA in the ternary complex is more blue-shifted, and the average lifetime becomes higher compared to the binary system. Circular dichroism spectral studies give information about the conformational changes of HSA in the absence and presence of GO when it forms complex with 7-DCA. The fluorescence lifetime imaging study shows the presence of the 7-DCA/HSA complex on the GO sheet. Molecular docking simulation shows that the closest distance between 7-DCA and HSA is 11.9 Å, and the protein interacted with the ligand through hydrogen bonding, hydrophobic interaction, and so forth.