Structural Compactness in Hen Egg White Lysozyme Induced by Bisphenol S: A Spectroscopic and Molecular Dynamics Simulation Approach

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.

Exploring the Noncovalent Interactions of the Dinuclear Cu(II) Schiff Base Complex with Bovine Serum Albumin and Cell Viability against the SiHa Cancer Cell Line

“…The CD spectra show an enhancement in ellipticity at ∼208 and ∼222 nm, respectively, which is associated with the helical nature of the protein. Upon addition of the complex, the increase in ellipticity for the helicity of BSA indicates that the presence of the complex makes the protein more compact and gives conformational stability . It is to be noted here that we could not record the CD spectra of BSA in the presence of the 60 μM complex (blue line in Figure ) beyond 218 nm, as the complex itself has a high absorption in this wavelength range (Figure a, inset), and also due to instrumental limitations.…”

Organo‐photocatalytic Synthesis of 6‐β‐Disubstituted Phenanthridines from α‐Diazo‐β‐Keto Compounds and Vinyl Azides

“…From all these observations, we can conclude that the actual quencher in this system is TBAB. Further, to ascertain the nature of quenching, we resorted to Stern‐Volmer analysis [16–18] . Herein, we explored the variation in fluorescence intensities of Rh‐6G in the presence of TBAB alone.…”

“…Further, to ascertain the nature of quenching, we resorted to Stern-Volmer analysis. [16][17][18] Herein, we explored the variation in fluorescence intensities of Rh-6G in the presence of TBAB alone. The fall in fluorescence intensity of Rh-6G with increasing concentrations of TBAB is depicted in Figure 1B.…”

Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa

“…The obtained ellipticity ( θ ) was expressed in MRE (Molar Residual Elipticity) and shown in Eq. (4) [ 36 ]: …”