Binding of naringin and naringenin with hen egg white lysozyme: A spectroscopic investigation and molecular docking study

Das, Sourav; Ghosh, Pooja; Koley, S.; Roy, Atanu Singha

doi:10.1016/j.saa.2017.11.015

Cited by 61 publications

(22 citation statements)

References 71 publications

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“…The difference spectra of [(HEWL+Chrysin)‐HEWL] showed that the characteristic peak maxima of chrysin (at 272 nm and 344 nm) decreased as compared to chrysin alone. These outcomes are supportive for the ground state complex formation between chrysin and HEWL that accounts for the involvement of static quenching mechanism ,,…”

Section: Resultssupporting

confidence: 55%

“…On binding with chrysin it was seen that the fluorescence intensity of peak 1 and 2 decreased with a corresponding increase in Stoke shift. The results obtained from the 3D fluorescence studies are listed in Table S1 and the increase in Stokes shift indicated the alteration in the HEWL conformation such that the polarity in the vicinity of Trp increased …”

Section: Resultsmentioning

confidence: 99%

“…As hen egg white lysozyme (HEWL) shares 60% sequence homology with human lysozyme, it has been utilized as a model protein for studying protein‐ligand interactions . Recently our group has reported the interactions of 7‐hydroxyflavone, 3‐hydroxyflavone, naringenin and naringin with HEWL ,. In recent times, the interaction studies of several small ligands with HEWL have been reported .…”

Section: Introductionmentioning

confidence: 99%

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Deciphering the Interaction of 5,7‐Dihydroxyflavone with Hen‐Egg‐White Lysozyme through Multispectroscopic and Molecular Dynamics Simulation Approaches

et al. 2018

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In recent times, research based on the bio‐active flavonoid, chrysin has shown its potential therapeutic applications such as anti‐diabetic, neuroprotective, anti‐asthmatic, anti‐depressant, etc. In order to understand its molecular recognition process, we studied its interaction with hen egg white lysozyme (HEWL) at physiological conditions. Chrysin (5,7‐Dihydroxyflavone) was able to quench the intrinsic fluorescence of HEWL through static quenching mechanism and the binding constant (Kb) was found to be (4.390±0.088 ×104) M−1 at 298 K and it decreased with the increase in temperature. The value of thermodynamic parameters such as ΔH (‐17.154±0.872) kJ mol−1 and ΔS (+31.267±3.151) J K−1 mol−1 indicated that hydrogen bonding and hydrophobic forces played a central role in the complexation process. Alteration in the Trp micro‐environment was induced due to the incorporation of chrysin in the binding site as indicated by synchronous and three dimensional (3D) fluorescence studies. FT‐IR and CD studies revealed that the secondary structure of HEWL was altered on chrysin binding, which resulted in an increase in the α‐helical stability of the protein. Chrysin inhibited the enzymatic activity of HEWL against M. lytus. Molecular docking and molecular simulation studies revealed that hydrogen bonding and hydrophobic forces played a vital role in complexation process. This study provides substantial insight into the binding of a bio‐active flavonoid (chrysin) with a carrier protein (HEWL).

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Section: Resultssupporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Deciphering the Interaction of 5,7‐Dihydroxyflavone with Hen‐Egg‐White Lysozyme through Multispectroscopic and Molecular Dynamics Simulation Approaches

et al. 2018

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“…values verify the spontaneous binding process in the interactions. 28 Thus, the data demonstrate the presence of only one binding site for MgO NPs in the HSA. Moreover, the K b values for MgO NPs show that the interaction of albumin with MgO NPs is very strong.…”

Section: Thermodynamic Parametersmentioning

confidence: 69%

“…The driving interactions between a NP and the protein include hydrophilic and hydrophobic forces. The thermodynamic parameters can be calculated by van't Hoff equation: 28 Ln…”

Section: Thermodynamic Parametersmentioning

confidence: 99%

Albumin binding and anticancer effect of magnesium oxide nanoparticles

Behzadi

Sarsharzadeh

Nouri

et al. 2018

IJN

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BackgroundRecently, nanomaterials have moved into biological and medicinal implementations like cancer therapy. Therefore, before clinical trials, their binding to plasma proteins like human serum albumin (HSA) and their cytotoxic effects against normal and cancer cell lines should be addressed.MethodsHerein, the interaction of magnesium oxide nanoparticles (MgO NPs) with HSA was studied by means of fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and docking studies. Afterwards, the cytotoxic impacts of MgO NPs on human leukemia cell line (K562) and peripheral blood mononucleated cells (PBMCs) were evaluated by MTT and flow cytometry assays to quantify reactive oxygen species (ROS) generation and apoptosis.ResultsIt was demonstrated that MgO NPs spontaneously form a static complex with HSA molecules through hydrophobic interactions. Docking study based on the size of NPs demonstrated that different linkages can be established between MgO NPs and HSA. The CD investigation explored that MgO NPs did not alter the secondary structure of HSA. Cellular studies revealed that MgO NPs induced cytotoxicity against K562 cell lines, whereas no adverse effects were detected on PBMCs up to optimum applied concentration of MgO NPs. It was exhibited that ROS production mediated by IC50 concentrations of MgO NPs caused apoptosis-associated cell death. The pre-incubation of K562 with ROS scavenger (curcumin) inhibited the impact of MgO NPs -based apoptosis on cell fate, revealing the upstream effect of ROS in our system.ConclusionIn summary, MgO NPs may exhibit strong plasma distribution and mediate apoptosis by ROS induction in the cancer cell lines. These data demonstrate a safe aspect of MgO NPs on the proteins and normal cells and their application as a distinctive therapeutic approach in the cancer treatment.

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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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Binding of naringin and naringenin with hen egg white lysozyme: A spectroscopic investigation and molecular docking study

Cited by 61 publications

References 71 publications

Deciphering the Interaction of 5,7‐Dihydroxyflavone with Hen‐Egg‐White Lysozyme through Multispectroscopic and Molecular Dynamics Simulation Approaches

Deciphering the Interaction of 5,7‐Dihydroxyflavone with Hen‐Egg‐White Lysozyme through Multispectroscopic and Molecular Dynamics Simulation Approaches

Albumin binding and anticancer effect of magnesium oxide nanoparticles

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

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