Binding Interaction of Juglone with Lysozyme: Spectroscopic Studies Aided by In Silico Calculations
Autor: | Joydeep Chowdhury, Saumen Saha |
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Rok vydání: | 2019 |
Předmět: |
Protein Conformation
alpha-Helical Circular dichroism 030303 biophysics Population Biophysics 02 engineering and technology Fluorescence spectroscopy 03 medical and health sciences chemistry.chemical_compound Radiology Nuclear Medicine and imaging education Protein secondary structure 0303 health sciences education.field_of_study Binding Sites Radiation Quenching (fluorescence) Radiological and Ultrasound Technology Chemistry Circular Dichroism Temperature Hydrogen Bonding 021001 nanoscience & nanotechnology Binding constant Molecular Docking Simulation Crystallography Spectrometry Fluorescence Thermodynamics Muramidase Lysozyme Time-resolved spectroscopy 0210 nano-technology Naphthoquinones Protein Binding |
Zdroj: | Journal of Photochemistry and Photobiology B: Biology. 193:89-99 |
ISSN: | 1011-1344 |
DOI: | 10.1016/j.jphotobiol.2019.02.006 |
Popis: | 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 α-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. |
Databáze: | OpenAIRE |
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