New exploration of the γ-gliadin structure through its partial hydrolysis - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue International Journal of Biological Macromolecules Année : 2020

New exploration of the γ-gliadin structure through its partial hydrolysis

Résumé

The partial enzymatic hydrolysis of wheat gliadins constitutes an interesting tool to unravel their structural specificity. In this work, the structure and conformation of γ-gliadin were investigated through its limited chymotrypsic digestion. Using a combination of computational, biochemical and biophysical tools, we studied each of its N and C terminal domains. Our results reveal that γ-gliadin is a partially disordered protein with an unfolded N-terminal domain surprisingly resistant to chymotrypsin and a folded C-terminal domain. Using spectroscopic tools, we showed that structural transitions occured over the disordered N-terminal domain for decreasing ethanol/water ratios. Using SAXS measurements, low-resolution 3D structures of γ-gliadin were proposed. To relate the repeated motifs of the N-terminal domain of γ-gliadin to its structure, engineered peptide models PQQPY/F were also studied. Overall results demonstrated similarities between the N-terminal domain and its derived model peptides. Our findings support the use of these peptides as general templates for understanding the wheat protein assembly and dynamics.
Fichier principal
Vignette du fichier
Sahli_27137.pdf (3.23 Mo) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)

Dates et versions

hal-03111116 , version 1 (15-01-2021)

Identifiants

Citer

Line Sahli, Adeline Boire, Véronique Solé-Jamault, Hélène Rogniaux, Alexandre Giuliani, et al.. New exploration of the γ-gliadin structure through its partial hydrolysis. International Journal of Biological Macromolecules, 2020, 165 (Part A), pp.654-664. ⟨10.1016/j.ijbiomac.2020.09.136⟩. ⟨hal-03111116⟩
100 Consultations
117 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More