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Deciphering the binding modes of hematoporphyrin to bovine serum albumin

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Title Deciphering the binding modes of hematoporphyrin to bovine serum albumin
 
Creator Ahmed, Mohammed
Guleria, Apurav
Singh, Ajay K
Bandyopadhyay, Tusar
Sarkar, Sisir K
 
Subject Fluorescence quenching
Bovine serum albumin
Hematoporphyrin
Fluorescence resonance energy transfer
Molecular docking
Molecular dynamics simulation
 
Description 175-187
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 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.
 
Date 2014-07-14T05:59:35Z
2014-07-14T05:59:35Z
2014-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/29092
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.51(3) [June 2014]