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Etude des propriétés interfaciales de l’Apolipoprotéine A-I : caractérisation de son organisation dans les films lipidiques de Langmuir

Abstract : This work belongs to the global study of interfacial properties of amphipathic repeats with Langmuir through. We work about Apolipoprotein A-I which belongs to the exchangeable apolipoprotein family. Proteins of this family are implied in cholesterol metabolism. Their sequences are mainly 11 amino-acids repeats, which form amphipathic α-helix for the formation of membrane around hydrophobic lipids. Ellipsometry, surface pressure measurements, IR spectroscopy (PM-IRRAS) and AFM microscopy were performed. We show that Apo A-I is inserted in LE phase (Expanded Liquid) of zwitterionic lipids (DPPC and DOPC), but is inserted in both LE and LC (Condensed Liquid) phases of anionic lipid (DPPG) with different conformation/orientation. Statistical analyses of form and spatial distribution of protein clusters over AFM images reveal that both charge and phase effects are present at the microscopic scale. On the basis of this microscopic study, we suggest an auto-assembling model for proteins organization in phospholipid monolayers. Finally, we compared Apo A-I with others proteins of the same family (Apo A-II) or others (Dystrophin sub-domains).
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https://tel.archives-ouvertes.fr/tel-03160137
Contributor : Lionel Chieze <>
Submitted on : Friday, March 5, 2021 - 1:51:11 AM
Last modification on : Sunday, March 7, 2021 - 3:07:51 AM

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  • HAL Id : tel-03160137, version 1

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Lionel Chieze. Etude des propriétés interfaciales de l’Apolipoprotéine A-I : caractérisation de son organisation dans les films lipidiques de Langmuir. Biophysique [physics.bio-ph]. Université de Rennes 1, 2009. Français. ⟨tel-03160137⟩

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