BARC/PUB/2014/0520

 
 

Deciphering the binding modes of hematoporphyrin to bovine serum albumin

 
     
 
Author(s)

Ahmed, M.; Guleria, A.; Singh, A. K.; Bandyopadhyay, T.; Sarkar, S. K.
(RPCD;TCS)

Source

Indian Journal of Biochemistry & Biophysics, 2014. Vol. 51 (3): pp. 175-187

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 ΔG0, ΔH0, and ΔS0 for the HP-BSA system which were -35.5 kJ mole-1, -56.4 kJ mole-1 and -0.06 kJ mole-1 K-1, respectively. These parameters suggested hydrogen-bonding and Van der Waals forces playing major role in the complexation. This was also supported by the bind ng energy parameters calculated by molecular docking. Moreover, the experimentally determined DG0 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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