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Approches biomimétiques de l'assemblage de protéines de réserve de blé

Abstract : Wheat storage proteins (prolamins) assembly in protein bodies during grain development still remains an ill-understood mechanism. This work displays different biomimetic strategies in order to elucidate physical chemistry parameters important for these proteins assembly in vivo. The g-gliadins and w-gliadins were chosen as model prolamins, and their assembly in aqueous solution was studied in vitro. This work focused on their interfacial behaviour. To mimic the biological context, these proteins were studied in the vicinity of lipidic membranes. Results indicate that, due to their low solubility, gliadins display an important ability to selfassemble in aqueous media, preferentially to the interfaces. Spectroscopic studies show that these proteins display labile secondary structures able to change their orientation at interfaces. In addition, at the air-water interface or under lipidic monolayers, gliadins adsorb to form protein monolayers. At high g-gliadins concentrations, the thickness of adsorbed protein layer increases to form dense protein domains, result not observed in the case of w-gliadins. A self assembly model, based on the primary structure of gliadins is thus proposed, and suggested as an initial mechanism of protein bodies formation.
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Contributor : Amélie Banc <>
Submitted on : Wednesday, December 1, 2010 - 6:01:39 PM
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  • HAL Id : tel-00542151, version 1



Amélie Banc. Approches biomimétiques de l'assemblage de protéines de réserve de blé. Biophysique []. Université Sciences et Technologies - Bordeaux I, 2007. Français. ⟨tel-00542151⟩



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