Luminescence,circular dichroism and in silico studies of binding interaction of synthesized naphthylchalcone derivatives with bovine serum albumin |
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Authors: | Sharda Pasricha Deepti Sharma Himanshu Ojha Pragya Gahlot Mallika Pathak Mitra Basu Raman Chawla Sugandha Singhal Anju Singh Rajeev Goel Shrikant Kukreti Shefali Shukla |
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Institution: | 1. Department of Chemistry, Sri Venkateswara College, University of Delhi, Delhi, India;2. Division of CBRN Defence, Institute of Nuclear Medicine and Allied Sciences, Delhi, India;3. Department of Chemistry, University of Delhi, Delhi, India;4. Nucleic Acid Research Laboratory, Department of Chemistry, University of Delhi, Delhi, India |
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Abstract: | Chalcones possess various biological properties, for example, antimicrobial, anti‐inflammatory, analgesic, antimalarial, anticancer, antiprotozoal and antitubercular activity. In this study, naphthylchalcone derivatives were synthesized and characterized using 1H NMR 13C NMR, Fourier transform infrared and mass techniques. Yields for all derivatives were found to be >90%. Protein–drug interactions influence the absorption, distribution, metabolism and excretion (ADME) properties of a drug. Therefore, to establish whether the synthesized naphthylchalcone derivatives can be used as drugs, their binding interaction toward a serum protein (bovine serum albumin) was investigated using fluorescence, circular dichroism and molecular docking techniques under physiological conditions. Fluorescence quenching of the protein in the presence of naphthylchalcone derivatives, and other derived parameters such as association constants, number of binding sites and static quenching involving confirmed non‐covalent binding interactions in the protein–ligand complex were observed. Circular dichroism clearly showed changes in the secondary structure of the protein in the presence of naphthylchalcones, indicating binding between the derivatives and the serum protein. Molecular modelling further confirmed the binding mode of naphthylchalcone derivatives in bovine serum albumin. A site‐specific molecular docking study of naphthylchalcone derivatives with serum albumin showed that binding took place primarily in the aromatic low helix and then in subdomain II. The dominance of hydrophobic, hydrophilic and hydrogen bonding was clearly visible and was responsible for stabilization of the complex. |
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Keywords: | bovine serum albumin circular dichroism docking luminescence quenching |
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