New exploration of the γ-gliadin structure through its partial hydrolysis - Archive ouverte HAL Access content directly
Journal Articles International Journal of Biological Macromolecules Year : 2020

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


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
Origin : Files produced by the author(s)

Dates and versions

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



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⟩
75 View
57 Download



Gmail Facebook Twitter LinkedIn More