Ahmed, MohammedGuleria, ApuravSingh, Ajay KBandyopadhyay, TusarSarkar, Sisir K2014-12-262014-12-262014-06Ahmed Mohammed, Guleria Apurav, Singh Ajay K, Bandyopadhyay Tusar, Sarkar Sisir K. Deciphering the binding modes of hematoporphyrin to bovine serum albumin. Indian Journal of Biochemistry & Biophysics. 2014 Jun; 51(3): 175-187.http://imsear.searo.who.int/handle/123456789/154221Interaction 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 G0, H0, and S0 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 binding energy parameters calculated by molecular docking. Moreover, the experimentally determined 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.enFluorescence quenchingBovine serum albuminHematoporphyrinFluorescence resonance energy transferMolecular dockingMolecular dynamics simulationAnimalsHematoporphyrins --chemistryHematoporphyrins --chemistryHematoporphyrins --metabolismKineticsMolecular Docking SimulationProtein BindingProtein ConformationSerum Albumin, Bovine --chemistrySerum Albumin, Bovine --metabolismSpectrometry, FluorescenceSpectroscopy, Fourier Transform InfraredThermodynamicsCattleArticle