Investigation of the Mechanism of 60 Co Gamma-Ray Irradiation-Stimulated Oxidation Enhancing the Antigenicity of Ovalbumin by High-Resolution Mass Spectrometry.
Zhong-Yue BianZong Cai TuHui WangYue-Ming HuGuang-Xian LiuPublished in: Journal of agricultural and food chemistry (2022)
60 Co gamma-ray irradiation-induced antigenicity changes in ovalbumin (OVA) were investigated, and the molecular mechanism was analyzed. Irradiation treatment at 0-100 kGy could significantly enhance the IgG/IgE binding ability of OVA in a dose-dependent paradigm by concomitant oxidative modification, which exhibited color browning and an increase in carbonyl content caused by high-penetrable rays. More allergenic epitopes of OVA were exposed after irradiation treatment reflected by structural changes including the unfolding of tertiary structure, the conversion of α-helix structures to β-sheet and random coil structures, and the cleavage of several peptide bonds. Meanwhile, three oxidation sites of K46, T49, and N260 located in key linear epitopes were observed, which might increase the allergenic ability of OVA via the disaggregation of noncovalent bonds and the unwinding of α-helix structures. Conclusively, irradiation may enhance the potential allergenicity of OVA by oxidative modification, which provides theoretical guidance for effectively controlling the oxidation of proteins in the irradiation process.
Keyphrases
- high resolution mass spectrometry
- high resolution
- dna binding
- radiation induced
- hydrogen peroxide
- liquid chromatography
- mass spectrometry
- oxidative stress
- risk assessment
- adipose tissue
- ms ms
- insulin resistance
- radiation therapy
- atomic force microscopy
- climate change
- gas chromatography
- electron transfer
- allergic rhinitis