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Caractérisation des puroindolines, des galactolipides du blé et de leurs interactions : mesures physiques aux interfaces

Abstract : Puroindolines (isoforms a and b) are proteins isolated from wheat seed. Their structure is stabilized by five disulfide bridges. Pin-a has a unique tryptophan-rich domain (WRWWKWWK). This domain is truncated in pin-b (WPTKWWK). Both major galactolipids from wheat endosperm, MGDG and DGDG, were extracted and purified. The studies have been performed at the air/liquid interface and in aqueous dispersion thanks to suitable techniques: tensiometry, ellipsometry, Brewster angle and atomic force microscopies, spectroscopic techniques (PM-IRRAS, Raman, ATR) and X-ray diffraction. The lipids and their equimolar mixture display specific properties attributed to strong interactions between the galactosyl polar headgroups. Pin-a and pin-b present similar properties, particularly a strong activity at the interface. Finally, the study of the protein/lipid interactions shows that pin-a interacts more strongly with the galactolipids by forming structures (networks) which could be the cause of the high stability of the foams of pin-a/lipid.
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Contributor : Celine Bottier <>
Submitted on : Tuesday, May 22, 2007 - 2:03:09 PM
Last modification on : Tuesday, January 12, 2021 - 4:39:35 PM
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  • HAL Id : tel-00148405, version 1

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Celine Bottier. Caractérisation des puroindolines, des galactolipides du blé et de leurs interactions : mesures physiques aux interfaces. Biophysique [physics.bio-ph]. Université Rennes 1, 2006. Français. ⟨tel-00148405⟩

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