Literature DB >> 25053052

IgE binding to peanut allergens is inhibited by combined D-aspartic and D-glutamic acids.

Si-Yin Chung1, Shawndrika Reed2.   

Abstract

The objective of this study was to determine if D-amino acids (D-aas) bind and inhibit immunoglobulin E (IgE) binding to peanut allergens. D-aas such as D-Asp (aspartic acid), D-Glu (glutamic acid), combined D-[Asp/Glu] and others were each prepared in a cocktail of 9 other D-aas, along with L-amino acids (L-aas) and controls. Each sample was mixed with a pooled plasma from peanut-allergic donors, and tested by ELISA (enzyme-linked immunosorbent assay) and Western blots for IgE binding to peanut allergens. Results showed that D-[Asp/Glu] (4 mg/ml) inhibited IgE binding (75%) while D-Glu, D-Asp and other D-aas had no inhibitory effect. A higher inhibition was seen with D-[Asp/Glu] than with L-[Asp/Glu]. We concluded that IgE was specific for D-[Asp/Glu], not D-Asp or D-Glu, and that D-[Asp/Glu] was more reactive than was L-[Asp/Glu] in IgE inhibition. The finding indicates that D-[Asp/Glu] may have the potential for removing IgE or reducing IgE binding to peanut allergens in vitro. Published by Elsevier Ltd.

Entities:  

Keywords:  Ara h 1 and Ara h 2; IgE antibodies; Peanut allergens; d-Amino acids; d-Aspartic acid; d-Glutamic acid

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Year:  2014        PMID: 25053052     DOI: 10.1016/j.foodchem.2014.06.004

Source DB:  PubMed          Journal:  Food Chem        ISSN: 0308-8146            Impact factor:   7.514


  2 in total

1.  Simple methods to reduce major allergens Ara h 1 and Ana o 1/2 in peanut and cashew extracts.

Authors:  Si-Yin Chung; Christopher P Mattison; Casey C Grimm; Shawndrika Reed
Journal:  Food Sci Nutr       Date:  2017-07-25       Impact factor: 2.863

Review 2.  Role of D-aspartate on biosynthesis, racemization, and potential functions: A mini-review.

Authors:  Yuying Li; Hui Han; Jie Yin; Tiejun Li; Yulong Yin
Journal:  Anim Nutr       Date:  2018-04-16
  2 in total

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