1. The mechanism of epigallocatechin-3-gallate inhibiting the antigenicity of β-lactoglobulin under pH 6.2, 7.4 and 8.2: Multi-spectroscopy and molecular simulation methods.
- Author
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Kuang, Xiaoyu, Deng, Zhifen, Feng, Bowen, He, Ran, Chen, Lang, and Liang, Guizhao
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MOLECULAR dynamics , *LACTOGLOBULINS , *EPIGALLOCATECHIN gallate , *FOURIER transform infrared spectroscopy , *ENZYME-linked immunosorbent assay , *CIRCULAR dichroism - Abstract
The antigenicity of β-lactoglobulin (β-LG) can be influenced by pH values and reduced by epigallocatechin-3-gallate (EGCG). However, a detailed mechanism concerning EGCG decreasing the antigenicity of β-LG at different pH levels lacks clarity. Here, we explore the inhibition mechanism of EGCG on the antigenicity of β-LG at pH 6.2, 7.4 and 8.2 using enzyme-linked immunosorbent assay, multi-spectroscopy, mass spectrometry and molecular simulations. The results of Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) elucidate that the noncovalent binding of EGCG with β-LG induces variations in the secondary structure and conformations of β-LG. Moreover, EGCG inhibits the antigenicity of β-LG the most at pH 7.4 (98.30 %), followed by pH 6.2 (73.18 %) and pH 8.2 (36.24 %). The inhibitory difference is attributed to the disparity in the number of epitopes involved in the interacting regions of EGCG and β-LG. Our findings suggest that manipulating pH conditions may enhance the effectiveness of antigenic inhibitors, with the potential for further application in the food industry. [Display omitted] • EGCG inhibited the antigenicity of β-LG in the order of pH 7.4 > 6.2 > 8.2. • EGCG reduced the antigenicity of β-LG by noncovalent binding. • EGCG binding to β-LG changed the secondary structure and conformation of β-LG. • EGCG binds to the outer surface of β-LG under three pH conditions. • The inhibitory effect of EGCG on β-LG antigenicity hinged on different binding sites. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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