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Interaction of Serum Albumins with Fluorescent Ligand 4-Azido Coumarin: Spectroscopic Analysis and Molecular Docking Studies

Abstract

The steady state fluorescence and time resolved fluorescence studies at 298K and low temperature phosphorescence (LTP) study at 77 K of the interaction of bovine serum albumin (BSA) and human serum albumin (HSA) with a ligand 4-azido-2H-chromen-2-one or 4-azidocoumarin (4-AC) have been carried out to visualize the location of the binding site and perturbation of the binding site of the tryptophan (Trp)/tyrosine (Tyr) of the protein (s) due to binding monitoring the emission maxima of Trp residue(s) in proteins. The estimation of fluorescence quenching study of Trp furnish that the binding constant for both the protein –ligand complexes is in the order of ~106 with binding site 1. The perturbation in the secondary structures of serum albumins due to binding of 4-AC are also observed from the circular dichroism (CD) studies. The energy transfer (ET) study further demonstrated that the non-radiative singlet-singlet ET takes place from Trp singlet states of proteins to singlet state of ligand is greater in case of BSA. This is supported by the distance and orientation of the donor-acceptor pair obtained from molecular docking studies. The molecular docking studies also fruitfully exploited to understand the involvement of Trp 213 in BSA and Trp 214 in HSA in the ET process along with the perturbation of the residues around 5 Å from the ligand 4-AC. Phosphorescence spectra at 77 K of Trp residues in the free proteins (BSA/HSA) and in the complexes of BSA/HSA have also been utilize to specify the role of Trp residues in ET and in the binding process.

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Publication details

The article was received on 04 Jul 2017, accepted on 03 Nov 2017 and first published on 03 Nov 2017


Article type: Paper
DOI: 10.1039/C7NJ02335A
Citation: New J. Chem., 2017, Accepted Manuscript
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    Interaction of Serum Albumins with Fluorescent Ligand 4-Azido Coumarin: Spectroscopic Analysis and Molecular Docking Studies

    S. Paul, N. Sepay, S. Sarkar, P. Roy, S. Dasgupta, P. Saha Sardar and A. MAJHI, New J. Chem., 2017, Accepted Manuscript , DOI: 10.1039/C7NJ02335A

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