Food Analytical Methods
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2015
·Vol. 8
·期 10
·2605-2611
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IF 1.956
Peng Juan,Song Shanshan,Liu Liqiang,Kuang Hua,Xu Chuanlai
In order to develop highly sensitive immunoassays for detecting the major peanut allergen, Ara h 2, we prepared six monoclonal antibodies (mAb) with high affinity to Ara h 2. Using mAb 5 as a capture antibody and HRP-labeled mAb 1 as a detection antibody, a sandwich enzyme-linked immunoassay (ELISA) was established with a limit of detection (LOD) of 0.02 ng/mL. An immunochromatographic strip based on these two mAbs was also established with a LOD of 1 ng/mL. Both tests showed high specificity in cross-reactivity experiments. Sample analyses indicated that these two immunoassays were feasible, accurate, and highly sensitive for measuring allergen Ara h 2 of food.
研究领域:
食品科学
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免疫学
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生物化学
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高影响因子
FOOD CHEMISTRY
·
2023
·
IF 8.8
Ping Yang,Xumei Wang,Hui Wang,Yueming Hu,Pingwei Wen,Zongcai Tu
The mechanism of the effect of reducing sugar chain length and isomers on the allergenicity of Ara h 2 after glycation was investigated. Ara h 2 was more prone to glycation with ribose which had a short chain length. The glycation sites of Ara h 2 after glycation with galactose were higher than the glycation sites in galactose’s isomers-Ara h 2 conjugates, which might be affected by the configuration differences at position C-4 and the small steric effects in terminal groups –CHO of galactose. Ara h 2-ribose conjugate had the lowest allergenicity, and glycation with galactose was more capable of reducing Ara h 2 allergenicity than its isomers. The results indicated that glycation with ribose caused conformational epitope destruction and linear epitope masking of Ara h 2 greatly. Furthermore, since the small steric effects of –CHO, galactose was more capable of reducing Ara h 2 allergenicity than fructose. This study will provide a theoretical basis for selecting appropriate reducing sugars and preparing hypoallergenic products containing peanuts.
研究领域:
食品科学
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过敏学
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生物化学
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PubMed
高影响因子
JOURNAL OF FOOD SCIENCE
·
2025
·Vol. 90
·期 8
·e70432
·
IF 3.4
Qin Geng,David Julian McClements,Taotao Dai,Wenlong Zhou,Zhihua Wu,Hongbing Chen
The molecular structure and surface properties of peanut proteins are altered by their non-covalent interactions with food polyphenols, which alter their allergenicity. In our research, the interactions between the critical peanut allergen (Ara h 2) and a model polyphenol (tannic acid [TA]) were studied utilizing experimental (spectroscopy and calorimetry) and molecular docking methods. Ultraviolet (UV) and circular dichroism (CD) spectroscopy analysis indicated that the microenvironment polarity and secondary/tertiary structure of Ara h 2 were changed due to its interaction with TA. Specifically, degree of molecular disorder increased, and the surface hydrophobicity of the polypeptide decreased after Ara h 2 interacted with TA. Analysis using fluorescence quenching, isothermal titration calorimetry, and molecular docking showed that the main non-covalent interactions were hydrogen bond formation between the Ara h 2 and TA. Binding site analysis using molecular docking indicated that the TA may have interacted with specific amino acids in the polypeptide chain, including Lys 31, Arg 34, Asp 35, Trp 44, Ser 54, Arg 59, Arg 60, Arg 122, Glu 123, and Gln 130. These amino acids are known to be part of the IgE epitope regions of Ara h 2, and so TA binding might be expected to impact peanut protein allergenicity. Indeed, an enzyme-linked immunosorbent assay (ELISA) study indicated that the IgE binding capacity of Ara h 2 was reduced after interacting with TA in a dose-dependent manner. This study enriches the understanding of the interactions between peanut protein allergens and small-molecule nutrients and provides a method for reducing the potential allergenicity of Ara h 2. Practical applications Employing the plant polyphenols as a means to modulate the activity of food allergens could potentially offer a breakthrough in managing food allergies. The strategic non-covalent binding of polyphenols, exemplified by TA, to the peanut allergen Ara h 2, may effectively lower its capacity to trigger allergic reactions, thereby offering an approach to mitigating peanut sensitization risks. The study examined the alterations in the structure and allergenic properties of Ara h 2 following its interaction with TA. This investigation was poised to accelerate the identification of TA's potential to inhibit peanut-induced allergic responses through allergen binding.
研究领域:
食品科学
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过敏研究
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分子生物学
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生物化学
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免疫学
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结构生物学
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高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2025
·
IF 6.2
Kuan Gao,Qin Geng,Changbao Hu,Wenhui Zhang,Xin Li,Ping Tong,Anshu Yang,Zhihua Wu,Hongbing Chen
Interactions between food allergens and polyphenols can provide a method to alleviate food allergies. This study investigated the effect of differently structured polyphenols complexed with Ara h 2 based on high-throughput virtual screening, utilizing a spectroscopic, thermodynamic, bone marrow-derived dendritic cells (BMDCs) model, BMDCs-T cells coculture model, KU812 cells model, and molecular simulation analyses for the allergenicity evaluation. Hesperidin (HSD), neohesperidin (NH), and neohesperidin dihydrochalcone (NHDC) exhibited a high binding energy and interacted with Ara h 2 through hydrogen bonding, primarily at two additional binding sites. This interaction led to protein unfolding and reduced hydrophobicity, particularly in the NH–Ara h2 complex. In addition, NH-bound Ara h2 has a lower potential for sensitization due to its reduced immunoglobulin E (IgE) binding capacity compared with Ara h 2 during gastrointestinal digestion. This is further supported by the decreased expression of costimulatory factors in BMDCs, the reduced release of allergenic cytokines, and the maintained balance of Th1, Th2, Th17, and Treg. The same trend was followed by the HSD and NHDC complexes. These findings suggest that glycosidic bond positions play a more significant role in reducing sensitization than does the flavonoid structure. Therefore, this study can assist in developing oral-specific immunotherapy of individuals with peanut allergies under the potential interaction mechanism of polyphenols and Ara h 2.
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高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2026
·
IF 6.2
Kuan Gao,Qin Geng,Wenhui Zhang,Xin Li,Ping Tong,Anshu Yang,Zhihua Wu,Hongbing Chen
The effects of pH-shifting combined with quercetin binding on peanut Ara h 2 were evaluated using multispectroscopy, cell models, molecular simulation, and correlation analysis. After dual treatment, Ara h 2 exhibited significant structural changes, as evidenced by decreased intrinsic fluorescence and converted α-helix into β-sheet, leading to reduced IgE-binding capacity and diminished ability of dendritic cells and T cells to differentiate toward the Th2 pathway due to the masking of epitopes. Moreover, the binding sites of quercetin gradually shifted toward the hydrophobic core of Ara h 2 with pH changes, which inhibited fluctuations in the aa50–70 region. Finally, according to the correlation analysis, pH-shifting combined with quercetin binding may reduce the allergenicity of Ara h 2 by the migration of many Trp and Tyr residues to the protein surface, which disrupted the conformational epitopes. Therefore, this study provides an approach for the development of hypoallergenic peanut products.
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高影响因子
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