Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols.
Autor: | Plundrich NJ; Plants for Human Health Institute, Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, North Carolina Research Campus, Kannapolis, NC 28081, USA., Cook BT; Department of Chemistry, Bioinformatics Research Center, North Carolina State University, Raleigh, NC 27695, USA., Maleki SJ; United States Department of Agriculture-Agricultural Research Service-Southern Regional Research Center, New Orleans, LA 70124, USA., Fourches D; Department of Chemistry, Bioinformatics Research Center, North Carolina State University, Raleigh, NC 27695, USA., Lila MA; Plants for Human Health Institute, Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, North Carolina Research Campus, Kannapolis, NC 28081, USA. Electronic address: mlila@ncsu.edu. |
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Jazyk: | angličtina |
Zdroj: | Food chemistry [Food Chem] 2019 Jun 30; Vol. 284, pp. 287-295. Date of Electronic Publication: 2019 Jan 18. |
DOI: | 10.1016/j.foodchem.2019.01.081 |
Abstrakt: | 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. (Copyright © 2019 Elsevier Ltd. All rights reserved.) |
Databáze: | MEDLINE |
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