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Structural Compactness in Hen Egg White Lysozyme Induced by Bisphenol S: A Spectroscopic and Molecular Dynamics Simulation Approach
- Source :
- ChemPhysChem. 22:1745-1753
- Publication Year :
- 2021
- Publisher :
- Wiley, 2021.
-
Abstract
- The endocrine disrupting compound Bisphenol and its analogues are widely used in food packaging products and can cause serious health hazards. The protein, Lysozyme (Lyz), showing anti-microbial properties, is used as a "natural" food and dairy preservative. Herein, we explored the interaction between Lyz and Bisphenol S (BPS) by multi-spectroscopic and theoretical approaches. Lyz interacts with BPS through static quenching, where hydrophobic force governed the underlying interaction. Molecular docking results reveal that tryptophan plays a vital role in binding, corroborated well with near UV-CD studies. A decrease in the radius of gyration (from 1.43 nm to 1.35 nm) of Lyz substantiates the compactness of the protein conformation owing to such an interaction. This structural alteration experienced by Lyz may alter its functional properties as a food preservative. Consequently, this can degrade the quality of the food products and thereby lead to severe health issues.
- Subjects :
- Bisphenol
Calorimetry
Molecular Dynamics Simulation
chemistry.chemical_compound
Molecular dynamics
Protein structure
Phenols
Endocrine disrupting compound
Animals
Benzhydryl Compounds
Physical and Theoretical Chemistry
Density Functional Theory
Binding Sites
Quenching (fluorescence)
Circular Dichroism
Temperature
Tryptophan
Atomic and Molecular Physics, and Optics
Molecular Docking Simulation
Spectrometry, Fluorescence
chemistry
Bisphenol S
Biophysics
Muramidase
Lysozyme
Chickens
Hydrophobic and Hydrophilic Interactions
Protein Binding
Subjects
Details
- ISSN :
- 14397641 and 14394235
- Volume :
- 22
- Database :
- OpenAIRE
- Journal :
- ChemPhysChem
- Accession number :
- edsair.doi.dedup.....0a47ac3b02ac3f3accc36c6b106bebc4