title: 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 deltaG0, deltaH0, and deltaS0 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 deltaG0 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.
authors.forename: Mohammed
authors.initials: M
authors.lastname: Ahmed
authors.forename: Apurav
authors.initials: A
authors.lastname: Guleria
authors.forename: Ajay K
authors.initials: AK
authors.lastname: Singh
authors.forename: Tusar
authors.initials: T
authors.lastname: Bandyopadhyay
authors.forename: Sisir K
authors.initials: SK
authors.lastname: Sarkar
mesh_terms: D000818:Animals; D002417:Cattle; D006415:Hematoporphyrins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D062105:Molecular Docking Simulation; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
chemical_list: D006415:Hematoporphyrins; C091193:haematoporphyrin-bovine serum albumin conjugate; D012710:Serum Albumin, Bovine