Interaction characterization of 5−hydroxymethyl−2−furaldehyde with human serum albumin: Binding characteristics, conformational change and mechanism

Zhou, Zhongwu; Hu, Xiaofeng; Hong, Xinyue; Zheng, Jie; Liu, Xia; Gong, Deming; Zhang, Guowen

doi:10.1016/j.molliq.2019.111835

Cited by 31 publications

(10 citation statements)

References 57 publications

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“…The fluorescence intensity of XO gradually decreased, while the absorption peaks of Tyr and Trp residues shifted slightly blue due to the increase in luteoloside concentration, as shown in Figure 5 52 . When the blue shift occurred, the polarity of protein amino acid residues decreased and the hydrophobicity increased, while the red shift was the opposite to the phenomenon of the blue shift 53 . Therefore, the results suggested that the polarity decreased and the hydrophobicity increased in the microenvironment of Tyr and Trp residue 54 .…”

Section: Resultsmentioning

confidence: 93%

“…52 When the blue shift occurred, the polarity of protein amino acid residues decreased and the hydrophobicity increased, while the red shift was the opposite to the phenomenon of the blue shift. 53 Therefore, the results suggested that the polarity decreased and the hydrophobicity increased in the microenvironment of Tyr and Trp residue. 54 Guo et al found that a slight blue-shift occurred when carnitine was added.…”

Section: Synchronous Fluorescence Spectramentioning

confidence: 96%

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Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Chen

Wang

Pan

et al. 2022

J of Molecular Recognition

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Gout is an inflammatory joint disease caused by urate crystal deposition, which is associated with hyperuricemia. Gout will take place when the uric acid accumulates. Xanthine oxidase (XO) is a crucial enzyme in the formation of uric acid. Inhibiting XO is one of the means to ameliorate gout. Luteoloside is a kind of natural flavonoid, which has an excellent prospect for relieving gout. But there are few reports on the interaction mechanism between luteoloside and XO currently. In this study, the interaction mechanism between luteoloside and XO was explored using spectroscopy and molecular docking. The fluorescence spectroscopy results indicated that luteoloside could make the intrinsic fluorescence of XO quenched, and the binding constant between luteoloside and XO was (1.85 ± 0.22) × 103 L mol−1 at 298 K. The synchronous fluorescence spectroscopy results showed that the absorption peaks of Tyr and Trp shifted blue, and the hydrophobicity of the microenvironment increased. Moreover, CD spectra showed that α‐helix of XO decreased, β‐sheet and β‐turn increased after adding luteoloside. The results of molecular docking analysis showed that XO could combine with luteoloside through hydrogen bonds and hydrophobic force. The results indicated that luteoloside could remarkably interact with XO. Insights into the interaction mechanism provide a necessary basis for the search for low‐toxic natural products as targets of XO. Highlights Luteoloside and xanthine oxidase was a strong binding mode and had only one binding site. Luteoloside could cause α‐helix reduced, β‐sheet and β‐turn increased, and change the secondary structure of XO. The binding between luteoloside and xanthine oxidase was a spontaneous process. The main binding force was hydrophobic force between luteoloside and xanthine oxidase.

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Section: Resultsmentioning

confidence: 93%

Section: Synchronous Fluorescence Spectramentioning

confidence: 96%

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Chen

Wang

Pan

et al. 2022

J of Molecular Recognition

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“…As shown in the 3D fluorescence spectra, the spectral feature of Trp and Tyr residues, which was due to the transition of π → π*, was mainly represented in peak a, and a characteristic fluorescence derived from the carbon skeleton of OVA was mainly reflected in peak b. 21 With the addition of RES to OVA, the fluorescence intensities of peaks a and b were significantly decreased, indicating that the binding of RES to OVA led to the conformational change of OVA. Besides, when the molar ratios of OVA to RES were 1:20, 1:50, and 1:100, there was a new peak in the spectra.…”

Section: Discussionmentioning

confidence: 93%

“…The synchronous fluorescence experiment, 3D fluorescence spectra measurement, and surface hydrophobicity assay were conducted using previous methods. [20][21][22] The detailed methods are described in the Supporting Information.…”

Section: Fluorescence Assaymentioning

confidence: 99%

Shedding light on the interaction of ovalbumin and resveratrol: structure, digestibility, transport, and allergenicity assessment of OVA–RES complexes

Xu,

Cao,

Yuan

et al. 2023

J Sci Food Agric

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BACKGROUNDThe interaction between food allergens and plant polyphenols has become a safe and effective management strategy to prevent food allergies. Ovalbumin (OVA) is the most abundant allergen in egg whites. Resveratrol (RES) is a plant polyphenol that is abundant in red grapes, berries, and peanuts and has an anti‐allergic effect on allergy‐related immune cells. However, there is little information about the effect of RES on the allergenicity of OVA. In this study, the effect of RES on the allergenicity of OVA was investigated.RESULTSThe molecular docking and spectroscopies indicated that the addition of RES changed the structure of OVA. The digestion and transfer rate of OVA‐RES were effectively improved with in vitro gastrointestinal digestion model and Caco‐2 cell model, especially when the molar ratio of OVA‐RES was 1:20. Meanwhile, the KU812 cell degranulation assay proved that the potential allergenicity was remarkably decreased while the molar ratios of OVA‐RES were increased to 1:20. Furthermore, hydrogen bonds and Van der Waals forces were the dominating force to stabilize the OVA‐RES complexes.CONCLUSIONSAll the findings demonstrated that the potential allergenicity of OVA was reduced when interacting with RES and RES can be a potential food material for preparing a hypoallergenic protein, especially for egg allergy.This article is protected by copyright. All rights reserved.

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“…3, the maximum emission wavelength of tyrosine and tryptophan residues decreased, and displayed a significant blue shift. Bindings can decrease the polarity around tyrosine and tryptophan residues and increase the hydrophobicity of tyrosine and tryptophan residues 46 . With increases of trans‐resveratrol, the fluorescence intensities of tyrosine and tryptophan residues decreased, and the fluorescence peaks of tyrosine residues showed a blue shift.…”

Section: Resultsmentioning

confidence: 99%

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

Liu

Chen

et al. 2021

J of Molecular Recognition

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It is an effective strategy to avoid obesity by inhibiting the activity of lipase. In this study, the binding mechanism of lipase and Lentinus edodes mycelia polysaccharide (LMP) were explored with multi‐spectral methods, for example, three‐dimensional (3D) fluorescence, Fourier‐transformed infrared (FT‐IR), and Raman spectra. At 290 K, the binding constant was 2.44 × 105 L/mol, there was only one binding site between LMP and lipase. Static quenching was the quenching mechanism. The major forces were hydrogen bonding and van der Waals force. The binding of LMP to lipase impacted the microenvironment around tyrosine and tryptophan residues. The polarity around these residues was decreased and hydrophobicity was enhanced. This study not only revealed the binding mechanism of LMP on lipase but also provided scientific evidence for expanding the application of LMP in functional food industries.

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Interaction characterization of 5−hydroxymethyl−2−furaldehyde with human serum albumin: Binding characteristics, conformational change and mechanism

Cited by 31 publications

References 57 publications

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Shedding light on the interaction of ovalbumin and resveratrol: structure, digestibility, transport, and allergenicity assessment of OVA–RES complexes

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

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