↓ Skip to main content

Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6; characterization of intermediate- and end products

Overview of attention for article published in Biochimica et Biophysica Acta (BBA), October 2013
Altmetric Badge

About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (92nd percentile)
  • High Attention Score compared to outputs of the same age and source (96th percentile)

Mentioned by

news
2 news outlets

Citations

dimensions_citation
45 Dimensions

Readers on

mendeley
51 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6; characterization of intermediate- and end products
Published in
Biochimica et Biophysica Acta (BBA), October 2013
DOI 10.1016/j.bbapap.2013.10.004
Pubmed ID
Authors

Danijela Apostolovic, Dion Luykx, Hans Warmenhoven, Dennis Verbart, Dragana Stanic-Vucinic, Govardus A.H. de Jong, Tanja Cirkovic Velickovic, Stef J. Koppelman

Abstract

Conglutins, the major peanut allergens, Ara h 2 and Ara h 6, are highly structured proteins stabilized by multiple disulfide bridges and are stable towards heat-denaturation and digestion. We sought a way to reduce their potent allergenicity in view of the development of immunotherapy for peanut allergy. Isoforms of conglutin were purified, reduced with dithiothreitol and subsequently alkylated with iodoacetamide. The effect of this modification was assessed on protein folding and IgE-binding. We found that all disulfide bridges were reduced and alkylated. As a result, the secondary structure lost α-helix and gained some β-structure content, and the tertiary structure stability was reduced. On a functional level, the modification led to a strongly decreased IgE-binding. Using conditions for limited reduction and alkylation, partially reduced and alkylated proteins were found with rearranged disulfide bridges and, in some cases, intermolecular cross-links were found. Peptide mass finger printing was applied to control progress of the modification reaction and to map novel disulfide bonds. There was no preference for the order in which disulfides were reduced, and disulfide rearrangement occurred in a non-specific way. Only minor differences in kinetics of reduction and alkylation were found between the different conglutin isoforms. We conclude that the peanut conglutins Ara h 2 and Ara h 6 can be chemically modified by reduction and alkylation, such that they substantially unfold and that their allergenic potency decreases.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 51 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 2%
Unknown 50 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 16 31%
Student > Master 9 18%
Researcher 8 16%
Student > Bachelor 3 6%
Student > Doctoral Student 2 4%
Other 2 4%
Unknown 11 22%
Readers by discipline Count As %
Agricultural and Biological Sciences 14 27%
Biochemistry, Genetics and Molecular Biology 7 14%
Medicine and Dentistry 5 10%
Immunology and Microbiology 5 10%
Engineering 3 6%
Other 4 8%
Unknown 13 25%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 20. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 12 August 2014.
All research outputs
#1,811,963
of 25,374,917 outputs
Outputs from Biochimica et Biophysica Acta (BBA)
#206
of 19,216 outputs
Outputs of similar age
#16,543
of 224,554 outputs
Outputs of similar age from Biochimica et Biophysica Acta (BBA)
#7
of 217 outputs
Altmetric has tracked 25,374,917 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 92nd percentile: it's in the top 10% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 19,216 research outputs from this source. They receive a mean Attention Score of 4.4. This one has done particularly well, scoring higher than 98% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 224,554 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 92% of its contemporaries.
We're also able to compare this research output to 217 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 96% of its contemporaries.