Scientific Study

Access to over 2,900 scientific references, studies and publications. This section is constantly updated with studies that have been published in scientific journals.

Back
Products: Peanuts

Notice: Undefined variable: post in /home/nimianet/domains/test.nimia.net/public_html/wp-content/mu-plugins/custom-studies.php on line 744

Notice: Trying to get property 'ID' of non-object in /home/nimianet/domains/test.nimia.net/public_html/wp-content/mu-plugins/custom-studies.php on line 744

Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols.

Authors: Plundrich, N. J., Cook, B. T., Maleki, S. J., Fourches, D., & Lila, M. A.
  • Journals: Food Chem
  • Pages: 287-295
  • Volume: 284
  • Year: 2019

Notice: Undefined variable: post in /home/nimianet/domains/test.nimia.net/public_html/wp-content/mu-plugins/custom-articles.php on line 247

Notice: Trying to get property 'ID' of non-object in /home/nimianet/domains/test.nimia.net/public_html/wp-content/mu-plugins/custom-articles.php on line 247
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.