Investigation on the binding behavior between BSA and lenvatinib with the help of various spectroscopic and in silico methods

Wang, Baoli; Kou, Song‐Bo; Lin, Zhen‐Yi; Shi, Jie‐Hua

doi:10.1016/j.molstruc.2019.127521

Cited by 76 publications

(25 citation statements)

References 37 publications

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“…Figure D shows the fitting of the data as per eq with the intercept of the plot giving the value of the binding constant ( K ) and the slope depicting the number of binding sites ( n ). The value of K was found to be 1.3 × 10 4 M –1 at 20 °C, indicating moderate binding between irisin and RT as has been reported for other protein–ligand interactions Table shows the K obtained at different temperatures, suggesting that a less stable complex is formed at higher temperatures as the value of K decreases at higher temperature.…”

Section: Resultssupporting

confidence: 63%

“…The value of K was found to be 1.3 × 10 4 M −1 at 20 °C, indicating moderate binding between irisin and RT as has been reported for other protein−ligand interactions. 46 Table 2 shows the K obtained at different temperatures, suggesting that a less stable complex is formed at higher temperatures as the value of K decreases at higher temperature.…”

Section: Interaction Study Between Purified Irisin and Rivastigmine T...mentioning

confidence: 99%

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Multispectroscopic and Molecular Docking Insight into Elucidating the Interaction of Irisin with Rivastigmine Tartrate: A Combinational Therapy Approach to Fight Alzheimer’s Disease

et al. 2021

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This study was aimed to study the interaction between purified irisin and rivastigmine tartrate (RT), a cholinesterase inhibitor used in Alzheimer's therapy. Irisin mainly promotes brown fat-like features in white adipose tissues; however, it has some important role in the nervous system also, i.e., capable of opposing synapse and memory failure in Alzheimer's disease (AD). The recombinant protein was purified by Ni−NTA chromatography and characterized using spectroscopic and in silico techniques. Further, the mechanism of interaction between irisin and RT was investigated using various biophysical techniques. Fluorescence quenching studies suggested that there exists a moderate binding between irisin and RT with a binding constant (K) of 10 4 M −1 and the irisin−RT complex is guided by a combination of both static and dynamic modes of quenching. Thermodynamic parameters suggested the reaction to be driven by hydrogen bonding, making it specific. FTIR and CD spectroscopy suggested no secondary structural alterations in irisin in the presence of RT. Molecular docking investigation provided an insight into the important residues that play a key role in irisin−RT interactions. This study delineates an important finding in AD therapy and can provide a platform further to explore the potential of irisin in AD treatment.

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Section: Resultssupporting

confidence: 63%

Section: Interaction Study Between Purified Irisin and Rivastigmine T...mentioning

confidence: 99%

Multispectroscopic and Molecular Docking Insight into Elucidating the Interaction of Irisin with Rivastigmine Tartrate: A Combinational Therapy Approach to Fight Alzheimer’s Disease

et al. 2021

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“…( 6 ) – ( 8 ). The average distance between BSA and MBZ is less than 8 nm suggesting that the energy transfer occurs 41 .…”

Section: Resultsmentioning

confidence: 99%

Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking

Gammal

Elmansi

El-Emam

et al. 2022

Sci Rep

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This article presents the binding interaction between mebendazole (MBZ) and bovine serum albumin. The interaction has been studied using different techniques, such as fluorescence quenching spectroscopy, UV–visible spectroscopy, synchronous fluorescence spectroscopy, fourier transform infrared, and fluorescence resonance energy transfer in addition to molecular docking. Results from Stern Volmer equation stated that the quenching for MBZ-BSA binding was static. The fluorescence quenching spectroscopic study was performed at three temperature settings. The binding constant (kq), the number of binding sites (n), thermodynamic parameters (ΔHο, ΔSο and ΔGο), and binding forces were determined. The results exhibited that the interaction was endothermic. It was revealed that intermolecular hydrophobic forces led to the stabilization of the drug-protein system. Using the site marker technique, the binding between MBZ and BSA was found to be located at subdomain IIA (site I). This was furtherly approved using the molecular docking technique with the most stable MBZ configuration. This research may aid in understanding the pharmacokinetics and toxicity of MBZ and give fundamental data for its safe usage to avoid its toxicity.

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“…Thus, the typical double logarithm equation is not suitable to calculate the binding constant for flavonoids on gliadin due to its specific situation that only static quenching occurs in the system, the quencher and the fluorophore are combined in a molar ratio of n : 1, and the quencher and the complex do not produce fluorescence in the measured wavelength range. Herein, to further discuss the binding affinity of flavonoids on gliadin, the equilibrium constant ( K a ) was calculated based on the assumption that both flavonoids and gliadin formed a 1 : 1 complex during the interaction: 28 where C 0 G and C 0 F are the initial concentration of gliadin and the flavonoid, respectively. C G is the free concentration of gliadin in the binding equilibrium system.…”

Section: Resultsmentioning

confidence: 99%

Insights from multi-spectroscopic analysis and molecular modeling to understand the structure–affinity relationship and the interaction mechanism of flavonoids with gliadin

Zhao

Huang

et al. 2022

Food Funct.

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Investigation on the binding behavior between BSA and lenvatinib with the help of various spectroscopic and in silico methods

Cited by 76 publications

References 37 publications

Multispectroscopic and Molecular Docking Insight into Elucidating the Interaction of Irisin with Rivastigmine Tartrate: A Combinational Therapy Approach to Fight Alzheimer’s Disease

Multispectroscopic and Molecular Docking Insight into Elucidating the Interaction of Irisin with Rivastigmine Tartrate: A Combinational Therapy Approach to Fight Alzheimer’s Disease

Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking

Insights from multi-spectroscopic analysis and molecular modeling to understand the structure–affinity relationship and the interaction mechanism of flavonoids with gliadin

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