Deciphering the binding modes of hematoporphyrin to bovine serum albumin

Abstract

Interaction of proteins with small molecules is important in understanding delivery and transport of different therapeutic agents, including drugs. In the present study, we investigated the interaction between hematoporphyrin (HP), the principal component of photosensitizing drug with bovine serum albumin (BSA) in aqueous buffer solution using UV-Vis absorption spectroscopy and fluorescence measurements. The results were further substantiated by molecular docking and molecular dynamics (MD) simulation. Our results revealed that fluorescence of BSA was dominantly quenched by the ground-state complex formation with HP accompanied by the electronic energy transfer (EET) to the later. We experimentally determined the thermodynamic parameters such as <img src='/image/spc_char/delta.gif' border=0>G⁰, <img src='/image/spc_char/delta.gif' border=0>H⁰, and <img src='/image/spc_char/delta.gif' border=0>S⁰ for the HP-BSA system which were -35.5 kJ mole^-1, -56.4 kJ mole^-1 and -0.06 kJ mole^-1K^-1, respectively. These parameters suggested hydrogen-bonding and Van der Waals forces playing major role in the complexation. This was also supported by the binding energy parameters calculated by molecular docking. Moreover, the experimentally determined <img src='/image/spc_char/delta.gif' border=0>G⁰ nicely correlated with those determined by molecular docking and MD-simulation. Further, computational results clearly showed that the binding of HP with BSA in the subdomains IB and IIA.

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