Targeting the heme protein hemoglobin by (−)-epigallocatechin gallate and the study of polyphenol–protein association using multi-spectroscopic and computational methods

Das, Sourav; Sarmah, Sharat; Hazarika, Zaved; Rohman, Mostofa Ataur; Sarkhel, Pallavi; Jha, Anupam Nath; Roy, Atanu Singha

doi:10.1039/c9cp05301h

Cited by 50 publications

(29 citation statements)

References 93 publications

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“…The trend in the obtained parameters from steady‐state experiments as listed in Table 1 infers an inverse dependence of K values on temperature. This observation is contrary to what we expect to encounter when static quenching is operational [29,30,32] . This result also opposed the observation made from UV‐Vis absorption study, where the increment of absorption (Figure 1a) led us to conclude the ground‐state complex formation between Lyz and BPS indicating the occurrence of static quenching mechanism [28,29,30] .…”

Section: Resultscontrasting

confidence: 99%

“…This observation is contrary to what we expect to encounter when static quenching is operational [29,30,32] . This result also opposed the observation made from UV‐Vis absorption study, where the increment of absorption (Figure 1a) led us to conclude the ground‐state complex formation between Lyz and BPS indicating the occurrence of static quenching mechanism [28,29,30] . However, the intriguing values of k q from Table 1 showed that it is higher than the maximum threshold value of k q for a diffusion‐controlled collision in an aqueous medium (∼10 10 M −1 s −1 ) for dynamic quenching process [30–32] .…”

Section: Resultscontrasting

confidence: 85%

“…An approach to understand the actual mechanism of the quenching process (static or dynamic) was to investigate the temperature dependent fluorescence behavior of Lyz induced by the addition of BPS. Faster diffusion at higher temperatures corresponds to a higher degree of dynamic quenching, whereas the opposite effect is the general trend in the case of static quenching [28,29,30] . To quantify the underlying quenching process between the fluorophore and the quencher, Stern‐Volmer equation was employed:

true \frac{F_{0}}{F} = 1 + K_{S V} ([], Q)

…”

Section: Resultsmentioning

confidence: 99%

“…To illustrate the actual scenario behind Lyz‐BPS interaction, the Arrhenius theory was used further. According to this theory, the rate constant is a function of temperature where the effect of temperature is pronounced in the static quenching process [30,33] . In dynamic quenching, k q should be less than 2×10 10 M −1 s −1 in an aqueous medium, whereas there is no upper limit in case of static quenching.…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2021

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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.

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Section: Resultscontrasting

confidence: 99%

Section: Resultscontrasting

confidence: 85%

true \frac{F_{0}}{F} = 1 + K_{S V} ([], Q)

…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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

et al. 2021

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“…They investigated the protein folding mechanism of villin with explicit solvation [42]. Apart from proteins, the technique has been extended to study other relevant biomolecules [43,44] and protein-nanoparticle interactions [45][46][47][48][49]. Simulation of any system revolves around lot of factors.…”

Section: Molecular Dynamics: the Computational Microscopementioning

confidence: 99%

Role of Force Fields in Protein Function Prediction

Hazarika¹,

Rajkhowa²,

Jha³

2021

Homology Molecular Modeling - Perspectives and Applications

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The world today, although, has developed an elaborate health system to fortify against known and unknown diseases, it continues to be challenged by new as well as emerging, and re-emerging infectious disease threats with severity and probable fluctuations. These threats also have varying costs for morbidity and mortality, as well as for a complex set of socioeconomic outcomes. Some of these diseases are often caused by pathogens which use humans as host. In such cases, it becomes paramount responsibility to dig out the source of pathogen survival to stop their population growth. Sequencing genomes has been finessed so much in the 21st century that complete genomes of any pathogen can be sequenced in a matter of days following which; different potential drug targets are needed to be identified. Structure modeling of the selected sequences is an initial step in structure-based drug design (SBDD). Dynamical study of predicted models provides a stable target structure. Results of these in-silico techniques greatly depend on force field (FF) parameters used. Thus, in this chapter, we intend to discuss the role of FF parameters used in protein structure prediction and molecular dynamics simulation to provide a brief overview on this area.

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Deciphering the interactions of phytochemicals with ovalbumin, the major food allergen from egg white: spectroscopic and computational studies

et al. 2022

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Ovalbumin (OVA), the major component of egg white, has been used as a model carrier protein to study the interaction of four bioactive phytochemicals 6-hydroxyflavone, chrysin, naringin, and naringenin. A static quenching mechanism was primarily associated with the complexation of the flavonoids with OVA. Hydrophobic forces play a major part in the stability of the complexes. The structural changes within the protein in response to flavonoid binding revealed a decrease in OVA's α-helical content. The hypothesized binding site for flavonoids in OVA overlaps with one or more immunoglobulin E-binding epitopes that may have some effect in the immunoglobulin E response pathway. The flavonoids remain in the same binding site throughout the simulation time and impart protein stability by forming different noncovalent interactions. This study presents comprehensive information about the interaction of the flavonoids with OVA and the associated structural variations after the binding, which might help researchers better comprehend similar medication pharmacodynamics and provide critical information for future therapeutic development.

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Targeting the heme protein hemoglobin by (−)-epigallocatechin gallate and the study of polyphenol–protein association using multi-spectroscopic and computational methods

Abstract: (−)-Epigallocatechin gallate binds to BHb and exhibits anti-glycating as well as antioxidant behaviors towards glycation and photo-oxidation of BHb.

Cited by 50 publications

References 93 publications

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

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

Role of Force Fields in Protein Function Prediction

Deciphering the interactions of phytochemicals with ovalbumin, the major food allergen from egg white: spectroscopic and computational studies

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