Plants for Human Health Institute, Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, North Carolina Research Campus, Kannapolis, NC 28081, USA.
Department of Chemistry, Bioinformatics Research Center, North Carolina State University, Raleigh, NC 27695, USA.
Food Chem. 2019 Jun 30;284:287-295. doi: 10.1016/j.foodchem.2019.01.081. Epub 2019 Jan 18.
The potential for 42 different polyphenols found in Vaccinium fruits to bind to peanut allergen Ara h 2 and inhibit IgE binding epitopes was investigated using cheminformatics techniques. Out of 12 predicted binders, delphinidin-3-glucoside, cyanidin-3-glucoside, procyanidin C1, and chlorogenic acid were further evaluated in vitro. Circular dichroism, UV-Vis spectroscopy, and immunoblotting determined their capacity to (i) bind to Ara h 2, (ii) induce protein secondary structural changes, and (iii) inhibit IgE binding epitopes. UV-Vis spectroscopy clearly indicated that procyanidin C1 and chlorogenic acid interacted with Ara h 2, and circular dichroism results suggested that interactions with these polyphenols resulted in changes to Ara h 2 secondary structures. Immunoblotting showed that procyanidin C1 and chlorogenic acid bound to Ara h 2 significantly decreased the IgE binding capacity by 37% and 50%, respectively. These results suggest that certain polyphenols can inhibit IgE recognition of Ara h 2 by obstructing linear IgE epitopes.
采用化学信息学技术研究了在越橘属水果中发现的 42 种不同多酚与花生过敏原 Ara h 2 结合并抑制 IgE 结合表位的潜力。在 12 种预测的结合物中，进一步评估了矢车菊素-3-葡萄糖苷、矢车菊素-3-葡萄糖苷、原花青素 C1 和绿原酸的体外结合能力。圆二色性、紫外可见光谱和免疫印迹法确定了它们（i）与 Ara h 2 结合的能力，（ii）诱导蛋白质二级结构变化的能力，以及（iii）抑制 IgE 结合表位的能力。紫外可见光谱清楚地表明原花青素 C1 和绿原酸与 Ara h 2 相互作用，圆二色性结果表明，与这些多酚的相互作用导致 Ara h 2 二级结构发生变化。免疫印迹表明，原花青素 C1 和绿原酸与 Ara h 2 结合显著降低了 37%和 50%的 IgE 结合能力。这些结果表明，某些多酚可以通过阻止线性 IgE 表位来抑制 Ara h 2 上 IgE 的识别。
