On the role of hydrophobic interactions between chloramphenicol and bovine pancreatic trypsin: The effect of a strong electrolyte

Pramanik, U. Datta; Khamari, Laxmikanta; Shekhar, Shashi; Mukherjee, Saptarshi

doi:10.1016/j.cplett.2020.137137

Cited by 20 publications

(47 citation statements)

References 46 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%

“…The raw heat change and the fittings at different temperatures are shown in Figure S7 and the calculated thermodynamic parameters are tabulated in Table S2. The positive values of ΔH and ΔS are clear signatures of the involvement of hydrophobic force [29,35,36] and the negative value of the free energy denotes the spontaneity of the interaction process. The trend in binding parameters was similar with that obtained from steady‐state analyses.…”

Section: Resultsmentioning

confidence: 99%

“…The trend in binding parameters was similar with that obtained from steady‐state analyses. However, a direct correlation between these two independent processes cannot be obtained as ITC reports a global picture of the interactive processes whereas, fluorescence reports the immediate microenvironment around the active fluorophore (here tryptophan) [29] …”

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%

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

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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Effect of Chloramphenicol as Antibiotic on the Structure and Function of Pepsin and Its Mechanism of Action

Wang,

Sun,

Nie

et al. 2023

Chemistry & Biodiversity

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The interaction between chloramphenicol (CHL) and pepsin (PEP), as well as the impact of CHL on PEP conformation, were investigated using spectroscopic techniques and molecular docking simulations in this study. The experimental results demonstrate that CHL exhibits a static quenching effect on PEP. The thermodynamic parameters indicate that the reaction between CHL and PEP is spontaneous, primarily driven by hydrogen bonding and van der Waals forces. Moreover, the binding distance of r<7 nm suggests the occurrence of Förster's non‐radiative energy transfer between these two molecules. In the synchronous fluorescence spectrum, the maximum fluorescence intensity of PEP produced a redshift phenomenon, indicating that CHL was bound to tryptophan residues of PEP. The addition of CHL induces changes in the secondary structure of PEP, as confirmed by the observed alterations in peak values in three‐dimensional fluorescence spectra. The UV spectra reveal a redshift of 3 nm in the maximum absorption peak, indicating a conformational change in the secondary structure of PEP upon addition of CHL. Circular dichroism analysis demonstrates significant alterations in the α‐helix, β‐sheet, β‐turn, and random coil contents of PEP before and after CHL incorporation, further confirming its ability to modulate the secondary structure of PEP.

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Macrocyclic Cavitand β‐Cyclodextrin Inhibits the Alcohol‐Induced Trypsin Aggregation

et al. 2022

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Trypsin, the most abundant pancreatic protein, aids in protein digestion by hydrolysis and exhibits aggregation propensity in presence of alcohol, which can further lead to pancreatitis and eventually pancreatic cancer. Herein, by several experimental and theoretical approaches, we unearth the inhibition of alcohol-induced aggregation of Trypsin by macrocyclic cavitand, β-cyclodextrin (β-CD). β-CD interacts with the native protein and shows inhibitory effect in a dose dependent manner. Moreover, the secondary structures and morphologies of Trypsin in presence of β-CD also clearly emphasize the inhibition of fibril formation. From Fluorescence Correlation Spectroscopy, we observed an enhancement in diffusion time of Nile Red with ~2.5 times increase in hydrodynamic radius, substantiating the presence of fibrillar structure. Trypsin also shows reduction in its functional activity due to alcohol-induced aggregation. Our simulation data reports the probable residues responsible for fibril formation, which was validated by molecular docking studies.

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On the role of hydrophobic interactions between chloramphenicol and bovine pancreatic trypsin: The effect of a strong electrolyte

Cited by 20 publications

References 46 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

Effect of Chloramphenicol as Antibiotic on the Structure and Function of Pepsin and Its Mechanism of Action

Macrocyclic Cavitand β‐Cyclodextrin Inhibits the Alcohol‐Induced Trypsin Aggregation

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