Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 193, Issue -, Pages 89-99Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2019.02.006
Keywords
Lysozyme; Juglone; Fluorescence spectroscopy; Molecular docking; Molecular dynamics
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Funding
- Department of Higher Education, Science & Technology and Biotechnology (DHESTB, Govt. of West-Bengal) [202 (Sanc.)/ST/P/S&T/16G-22/2017 03(7471)/18]
- Council of Scientific and Industrial Research (CSIR) [202 (Sanc.)/ST/P/S&T/16G-22/2017 03(7471)/18]
- UGC, Government of India
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Binding interactions between the drug Juglone (JUG) and Lysozyme (LYZ) have been explored in details from spectroscopic studies aided by in silico calculations. UV-Vis, steady state and time resolved fluorescence spectroscopic studies indicate the formation of LYZ-JUG complex in the ground state. Quenching of corrected fluorescence spectra of LYZ in presence of JUG at varied concentrations in different temperature range have been estimated from Stern-Volmer (SV) plots. Time resolved fluorescence spectroscopic studies confirm the mechanism of quenching to be of static type. Binding constant associated with the LYZ-JUG complex has been estimated from Scatchard plot. The number of binding sites, thermodynamic parameters and the modes of interaction are also estimated. Synchronous fluorescence spectra monitored at two discrete wavelength windows confirm the prominent role of Tryptophan residues towards quenching of fluorescence in LYZ. The circular dichroism (CD) spectra signify alterations in the population of alpha-helical content within the secondary structure of LYZ in presence of JUG molecules. REES of LYZ in the presence of JUG further signify definite impact of the drug JUG molecule on the Trp residues of the protein. The experimental observations are supported by in silico molecular docking and molecular dynamics simulations.
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