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

Abstract : 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.
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Submitted on : Friday, January 15, 2021 - 10:02:52 AM
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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, Elsevier, 2020, 165 (Part A), pp.654-664. ⟨10.1016/j.ijbiomac.2020.09.136⟩. ⟨hal-03111116⟩



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