INCREASED HLA-DQ2-AFFINITY OF A SYNTHETIC GLIADIN PEPTIDE BY ACID-INDUCED DEAMIDATION OF GLUTAMINE RESIDUES

Authors
TERREAUX C WALK T VANDEWAL Y KONING F JUNG G FLECKENSTEIN B
Citation
C. Terreaux et al., INCREASED HLA-DQ2-AFFINITY OF A SYNTHETIC GLIADIN PEPTIDE BY ACID-INDUCED DEAMIDATION OF GLUTAMINE RESIDUES, Bioorganic & medicinal chemistry letters, 8(15), 1998, pp. 2039-2044
Citations number
14
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
8
Issue
15
Year of publication
1998
Pages
2039 - 2044
Database
ISI
SICI code
0960-894X(1998)8:15<2039:IHOASG>2.0.ZU;2-D
Abstract
Presentation of antigenic gliadin peptides by the HLA-DQ2 molecule is considered as a key event in celiac disease pathogenesis. Chemical dea midation of the side chains of glutamine residues might have a strong influence on gliadin peptide binding to the DQ2 molecule. Glutamine de amidation of A-gliadin peptide (45-56) under acidic conditions corresp onding to the gastric environment was studied using RP-HPLC, Edman deg radation, capillary electrophoresis and electrospray mass spectrometry . Deamidation resulted in peptides with increased DQ2-affinities as as sessed in a cell-free binding assay. (C) 1998 Elsevier Science Ltd. Al l rights reserved.