Spectroscopic and in silico insight into the interaction between dicofol and human serum albumin

Li, Na; Yang, Xi; Chen, Fengping; Zeng, Guofang; Zhou, Like; Li, Xiaoke; Tuo, Xun

doi:10.1016/j.saa.2021.120277

Cited by 23 publications

(2 citation statements)

References 53 publications

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“…These results implied that the distance between NDP and Trp residues was shorter than between NDP and Tyr. [56] Furthermore, there was a slightly red shift in the Tyr maximum emission bands (from 288 nm to 289 nm), whereas the fluorescence intensity of Trp showed almost no change. These results indicated that NDP could change the microenvironment around the Tyr and the Tyr residues that tended to be buried in a more hydrophilic environment.…”

Section: Confirmed the Binding Informationmentioning

confidence: 97%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

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Nifedipine (NDP), a dihydropyridine calcium antagonist, is widely used for the treatment of hypertension and angina pectoris. Catalase is a key antioxidant enzyme that is closely relevant to the level of reactive oxygen specie in vivo. Here, the research explored the effects of NDP on the conformation and catalytic function of bovine liver catalase (BLC) through enzymatic reaction kinetic techniques, multispectroscopic analysis, and computer simulation methods. Kinetic studies clarified that the NDP reduced the activity of BLC using a noncompetitive inhibition mechanism.Based on trial data, a static quenching mechanism functioned in quenching the intrinsic fluorescence of BLC. The binding constant value was (4.486 ± 0.008) Â 10 4 M À1 (298 K) and BLC had one binding site for NDP. Tyr was prone to be exposed more to a hydrophilic environment in wake of a shift in fluorescence value. The binding reaction of BLC to NDP caused a conformational change in BLC, which in turn led to

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Section: Confirmed the Binding Informationmentioning

confidence: 97%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

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“…Through the analysis of various structural parameters, the binding model of ligand-protein complexes can be predicted and the results can be visualized. [51] To more fully explain the binding of CBZ to BSA, we conducted molecular docking to predict their binding sites and minimum binding energies. [52] Molecular docking simulation demonstrates that the binding region of CBZ and BSA is located in the hydrophobic region of Site I, which is consistent with the site competition replacement experiment.…”

Section: Molecular Dockingmentioning

confidence: 99%

The influence of several nutritional supplements on the rational use of cabozantinib

Duan

Wang²,

Liu

et al. 2022

Luminescence

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To promote the rational use of cabozantinib (CBZ), this paper studied the influence of several nutritional supplements on the interaction between CBZ and bovine serum albumin (BSA), an appropriate alternative model for human serum albumin (HSA) that is one of the important transporter proteins in plasma, by fluorescence spectroscopy and UV–vis spectroscopy. The results showed that CBZ could quench the fluorescence of BSA via a dynamic–static quenching process, and the six nutritional supplements did not change the quenching mode of BSA by CBZ. However, all of them could reduce the binding constant of the CBZ–BSA system at 293 K and increase the polarity around tryptophan residues. Among them, nicotinamide and vitamin B12 (VB12) had a greater effect on the binding constants of the CBZ–BSA system. In the meantime, the thermodynamic parameters of the CBZ–BSA system were examined, indicating that the interaction of CBZ with BSA was spontaneous and dominated by hydrophobic forces. Further research discovered that the combining of CBZ with BSA was primarily located within Site I of BSA, and the binding distance r was 2.48 nm. Consequently, while taking CBZ, patients should use VB12 and nicotinamide carefully, which may interfere with the transport of drugs.

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A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Hashemizadeh

Shiri

Shahraki

et al. 2022

Applied Organom Chemis

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Catalase (CAT) is an essential protein protecting the cell from oxidative damage by reactive oxygen species. CAT is a heme enzyme in which iron metal plays a crucial role in catalytic activity. In this research, an iron (II, III) complex ([Fe (bpy) 3 ] [Fe (dipic) 2 ] 2 .7H 2 O; dipic À2 = pyridine-2,6-dicarboxylato and bpy = 2,2 0 -bipyridine) was used to evaluate its binding interactions with bovine liver catalase (BLC) using spectroscopic and molecular docking methods. The experimental results demonstrated that the catalytic activity of BLC increased slightly and reached 106% of the initial activity. The interactions between Fe complex and BLC led to the quenching of the catalase fluorescence emission via the static quenching mechanism. Thermodynamic parameters demonstrated that the predominant interactions between catalase and Fe complex are hydrogen bond and van der Waals and the process is exothermic and enthalpy driven. The circular dichroism (CD) and synchronous fluorescence results showed that the Fe complex altered the structure and conformation of BLC. It changed the secondary structure of BLC by decreasing α-helix and β-sheet content. Also, the experimental data were analyzed using Multivariate Curve Resolution-Alternating Least Square (MCR-ALS) to the resolution of measured complex spectra and estimate the number of independent chemical species. The docking results in agreement with experimental data showed that the cationic part of the complex with catalase is mainly hydrophobic and van der Waals interactions, and for the anionic part are hydrophobic, van der Waals, and hydrogen bonding.

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Spectroscopic and in silico insight into the interaction between dicofol and human serum albumin

Cited by 23 publications

References 53 publications

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

The influence of several nutritional supplements on the rational use of cabozantinib

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

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