Structural Compactness in Hen Egg White Lysozyme Induced by Bisphenol S: A Spectroscopic and Molecular Dynamics Simulation Approach.
Ushasi PramanikAnju Ajayan KongasseriShashi ShekharAshwin MathewRahul YadavSaptarshi MukherjeePublished in: Chemphyschem : a European journal of chemical physics and physical chemistry (2021)
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.
Keyphrases
- molecular docking
- molecular dynamics simulations
- human health
- public health
- healthcare
- mental health
- binding protein
- photodynamic therapy
- risk assessment
- health information
- microbial community
- protein protein
- amino acid
- small molecule
- genome wide
- gene expression
- early onset
- quantum dots
- ionic liquid
- social media
- case control
- dna binding