Репозиторијум Хемијског факултета - Cherry
Универзитет у Београду - Хемијски факултет
    • English
    • Српски
    • Српски (Serbia)
  • Српски (ћирилица) 
    • Енглески
    • Српски (ћирилица)
    • Српски (латиница)
  • Пријава
Преглед рада 
  •   Репозиторијум Хемијског факултета - Cherry
  • Hemijski fakultet
  • Radovi
  • Преглед рада
  •   Репозиторијум Хемијског факултета - Cherry
  • Hemijski fakultet
  • Radovi
  • Преглед рада
JavaScript is disabled for your browser. Some features of this site may not work without it.

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

Само за регистроване кориснике
2013
1461.pdf (1.336Mb)
Аутори
Apostolovic, Danijela
Luykx, Dion
Warmenhoven, Hans
Verbart, Dennis
Stanić-Vučinić, Dragana
de Jong, Govardus A. H.
Ćirković-Veličković, Tanja
Koppelman, Stef J.
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документу
Апстракт
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 allcylated 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 a-helix and gained some beta-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 fi...nger 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. (C) 2013 Elsevier B.V. All rights reserved.

Кључне речи:
Allergen / Mass spectrometry (MS) / Peanut / Spectroscopy / Immunochemistry / Protein structure
Извор:
Biochimica et Biophysica Acta: Proteins and Proteomics, 2013, 1834, 12, 2832-2842
Издавач:
  • Elsevier Science Bv, Amsterdam
Пројекти:
  • Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-172024)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)

DOI: 10.1016/j.bbapap.2013.10.004

ISSN: 1570-9639

PubMed: 24145103

WoS: 000329418300040

Scopus: 2-s2.0-84887391859
[ Google Scholar ]
URI
http://cherry.chem.bg.ac.rs/handle/123456789/1463
Колекције
  • Radovi
Институција
Hemijski fakultet

DSpace software copyright © 2002-2015  DuraSpace
О Cherry репозиторијуму | Пошаљите запажања

OpenAIRERCUB
 

 

Комплетан репозиторијумИнституцијеАуториНасловиТемеОва институцијаАуториНасловиТеме

DSpace software copyright © 2002-2015  DuraSpace
О Cherry репозиторијуму | Пошаљите запажања

OpenAIRERCUB