Spectroscopic study on the interaction of Trypsin with Bicyclol and analogs

Zhang

2014

J. Agric. Food Chem.

Dimethyl phthalate (DMP) is widely used as a plasticizer in industrial processes and has been reported to possess potential toxicity to the human body. In this study, the interaction between DMP and trypsin in vitro was investigated. The results of fluorescence, UV–vis, circular dichroism, and Fourier transform infrared spectra along with cyclic voltammetric measurements indicated that the remarkable fluorescence quenching and conformational changes of trypsin resulted from the formation of a DMP–trypsin complex, which was driven mainly by hydrophobic interactions. The molecular docking and trypsin activity assay showed that DMP primarily interacted with the catalytic triad of trypsin and led to the inhibition of trypsin activity. The dimensions of the individual trypsin molecules were found to become larger after binding with DMP by atomic force microscopy imaging. This study offers a comprehensive picture of DMP–trypsin interaction, which is expected to provide insights into the toxicological effect of DMP.

Section: Introductionmentioning

confidence: 99%

Potential Toxicity of Phthalic Acid Esters Plasticizer: Interaction of Dimethyl Phthalate with Trypsin in Vitro

Zhang

2014

J. Agric. Food Chem.

“…Furthermore, K a1 values for CYP3A4–astilbin, CYP3A4–isoastilbin, and CYP3A4–neoastilbin diminished quickly with the increase in temperature. Therefore, the increase in the instability of the complex formed by three flavonoids and CYP3A4 at a relatively high temperature was elucidated [35]. Moreover, astilbin had the strongest binding ability with CYP3A4, followed by isoastilbin and neoastilbin according to the corresponding K a1 at the same temperature.…”

Section: Resultsmentioning

confidence: 99%

Comparative study of the interaction mechanism of astilbin, isoastilbin, and neoastilbin with CYP3A4

Tao,

Fan,

Wang

et al. 2023

Luminescence

The interactions of human CYP3A4 with three selected isomer flavonoids, such as astilbin, isoastilbin and neoastilbin, were clarified using spectral analysis, molecular docking, and molecular dynamics simulation. During binding with the three flavonoids, the intrinsic fluorescence of CYP3A4 was statically quenched in static mode with nonradiative energy conversion. The fluorescence and ultraviolet/visible (UV/vis) data revealed that the three flavonoids had a moderate and stronger binding affinity with CYP3A4 due to the order of the Ka1 and Ka2 values ranging from 104 to 105 L·mol−1. In addition, astilbin had the highest affinity with CYP3A4, then isoastilbin and neoastilbin, at the three experimental temperatures. Multispectral analysis confirmed that binding of the three flavonoids resulted in clear changes in the secondary structure of CYP3A4. It was found from fluorescence, UV/vis and molecular docking analyses that these three flavonoids strongly bound to CYP3A4 by means of hydrogen bonds and van der Waals forces. The key amino acids around the binding site were also elucidated. Furthermore, the stabilities of the three CYP3A4 complexes were evaluated using molecular dynamics simulation.

J of Molecular Recognition

“…Three‐dimensional fluorescence spectroscopy technology completely display the fluorescence information . 55 The three‐dimensional fluorescence spectra of FTO‐acrylonitrile derivatives are shown in Figure 7 and Figure S7. The fluorescence peak at 280 nm is mainly spectral characteristics of tryptophan and tyrosine residues.…”

Section: Resultsmentioning

confidence: 99%

The role of chlorine atom on the binding between acrylonitrile derivatives and fat mass and obesity‐associated protein

Bai

Gan

et al. 2020

Self Cite

In this work, seven acrylonitrile derivatives were selected as potential inhibitors of fat and obesity‐related proteins (FTO) by the aid of fluorescence spectroscopy, ultraviolet visible spectroscopy, molecular docking, and cytotoxicity methods. Results show that the interaction between 3‐amino‐2‐(4‐chlorophenyl)‐3‐phenylacrylonitrile (1a) and FTO was the strongest among these derivatives. Thermodynamic analysis and molecular modeling show that the main force between 1a and FTO is hydrophobic interaction. The cytotoxicity test showed that the IC50 value of 1a was 46.64 μmol/L, which indicated 1a had the smallest IC50 value and had the best inhibitory effect on the proliferation of leukemia K562 cells among the seven derivatives. Both our previous results and this work show that chlorine atoms play important role in the binding of small molecules and FTO. This work brings new information for the study of FTO inhibitors.