Superoxide dismutase response and the underlying molecular mechanism induced by iodoacetic acid

Wang, Jing; Jia, Rui; Zheng, Xiaolin; Liu, Rutao; Zong, Wansong

doi:10.1016/j.chemosphere.2019.06.108

Cited by 28 publications

(4 citation statements)

References 49 publications

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“…The strong absorption peak at 208 nm is related to the protein backbone, which is caused by the π-π* transition of C=O in the polypeptide chain backbone associated with helix-coil transformation; the peak at 280 nm is related to the absorption of aromatic amino acids. 37,38 As shown in Fig. 3, as the concentration of DHA-S increased, the absorption intensity of HSA at 208 nm was continuously weakened with a slight red shift, but the characteristic absorption peak of aromatic amino acids near 280 nm did not change significantly.…”

Section: Resultsmentioning

confidence: 91%

“…3 we can see that HSA has two absorption peaks (at about 208 nm and 280 nm). The strong absorption peak at 208 nm is related to the protein backbone, which is caused by the π‐π* transition of C=O in the polypeptide chain backbone associated with helix‐coil transformation; the peak at 280 nm is related to the absorption of aromatic amino acids 37,38 . As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

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Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Cui

Xiao

et al. 2021

J Sci Food Agric

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BACKGROUND: Sodium dehydroacetate (DHA-S) is a common food additive, which can combine with serum proteins in the plasma, but the interaction mechanism between DHA-S and human serum albumin (HSA) is unclear. In this study, multiple spectroscopy techniques, isothermal titration calorimetry (ITC), molecular docking and esterase activity test were employed to investigate the interaction mechanism of DHA-S and HSA. RESULTS: A DHA-S-HSA complex was formed and the structure of HSA were altered by DHA-S. Since DHA-S changed the tight structure of the hydrophobic subdomain IIA where tryptophan (Trp) was placed, the hydrophobicity of the microenvironment of HSA was enhanced. With the addition of DHA-S, the skeleton structure of HSA became loose and the solvent shell on the HSA surface was destroyed. DHA-S altered the secondary structure of HSA, resulting in the decreased ⊍-helix and increased ⊎-sheet contents. The interaction was exothermic and spontaneous driven by van der Waals and hydrogen bonding. DHA-S inhibited the esterase activity of HSA. Molecular docking demonstrated that the binding site of DHA-S on HSA located at the cavity of subdomains IIA and IIIA, but the amino acids related to esterase activity of HSA were not in the binding pocket, indicating that the mechanism by which DHA-S inhibited HSA esterase activity was the change in protein structure.CONCLUSION: This study illustrated that DHA-S interacted with HSA and the structure and function of HSA were affected by DHA-S. This research could help to understand the toxicity of DHA-S and provide basic data for safe use of food additives.

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Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Cui

Xiao

et al. 2021

J Sci Food Agric

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“…The value of ΔH was much less than 60 kcal m −1 , indicating that the interaction between IND and SOD was non-covalent [ 46 ]. When the ligand-protein interaction was strong, the binding constant (K) was usually between 10 7 and 10 8 [ 47 , 48 ]. The order of magnitude of K IND-SOD was 10 3 , indicating that the binding affinity between IND and SOD was relatively weak.…”

Section: Resultsmentioning

confidence: 99%

“…The change of SOD structure and conformation may be affected by the change of protein particle size after IND binding [ 47 , 54 ]. Resonant light scattering (RLS) spectroscopy was used to study the particle size changes of the system before and after IND exposure.…”

Section: Resultsmentioning

confidence: 99%

Cytotoxicity and Oxidative Stress Effects of Indene on Coelomocytes of Earthworm (Eisenia foetida): Combined Analysis at Cellular and Molecular Levels

Huo

Qiang²,

Liu

et al. 2023

Toxics

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Indene (IND) is a kind of important aromatic hydrocarbon that is extracted from coal tar and has important applications in industry and biology. In the process of production and utilization, it is easy to enter the soil and produce toxic effects on the soil or organisms. The earthworm is an important organism in the soil. The toxicity of indene on earthworm coelomocytes is rarely studied, and the oxidative stress effects of IND on earthworm coelomocytes remain unclear. In this study, coelomocytes from earthworms and antioxidant enzymes were selected as the research targets. In addition, IND caused oxidative stress, and its related toxic effects and mechanisms were systematically studied and evaluated at the cellular and molecular levels. The results showed that IND destroyed the redox balance in earthworm coelomocytes, and the large accumulation of reactive oxygen species (ROS) significantly inhibited the activities of the antioxidant system, including superoxide dismutase (SOD), catalase (CAT), and glutathione (GSH), and caused lipid peroxidation and membrane permeability changes, resulting in a decrease in cell viability to 74.5% of the control group. At the molecular level, IND was bound to SOD by the arene-H bond, and the binding constant was 4.95 × 103. IND changed the secondary structure of the SOD and led to a loosening of the structure of the SOD peptide chain. Meanwhile, IND caused SOD fluorescence sensitization, and molecular simulation showed that IND was mainly bound to the junction of SOD subunits. We hypothesized that the changes in SOD structure led to the increase in SOD activity. This research can provide a scientific basis for IND toxicity evaluation.

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Molecular interaction mechanisms and cellular response of superoxide dismutase and catalase to fluoranthene

Song,

Sun,

Zhao

et al. 2023

Environ Sci Pollut Res

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Superoxide dismutase response and the underlying molecular mechanism induced by iodoacetic acid

Cited by 28 publications

References 49 publications

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Cytotoxicity and Oxidative Stress Effects of Indene on Coelomocytes of Earthworm (Eisenia foetida): Combined Analysis at Cellular and Molecular Levels

Molecular interaction mechanisms and cellular response of superoxide dismutase and catalase to fluoranthene

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