Structure, Orientation and Stability of Lysozyme Confined in layered Materials

Sébastien Balme 1 Régis Guégan 2 Jean-Marc Janot 1 Maguy Jaber 3 Mathilde Lepoitevin 1 Philippe Dejardin 1 Xavier Bourrat 2 Mikael Motelica-Heino 2
1 ICGM ICMMM - Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier
2 ISTO - Institut des Sciences de la Terre d'Orléans - UMR7327
3 LRS - Laboratoire de Réactivité de Surface
Abstract : The confinement of lysozyme in 3 layered materials based on montmorillonite and lamellar double hydroxide exhibiting different surface charges was studied. The protein structure and orientation in these materials were determined by X-Ray diffraction, time resolved fluorescence and fluorescence anisotropy. For both Montmorillonite exchanged with sodium and modified with non-ionic surfactant (tri-ethylene glycol mono n-decyl ether), the lysozyme was found to be located in the interlayer space with "end-on" and "side-on" orientation, respectively. Conversely no lysozyme intercalation was observed with lamellar double hydroxide modified with anionic surfactant (sodium octylsulfate), since protein was adsorbed on the surface of the particles. Fourier transformed infra-red spectroscopy analysis shows that lysozyme confinement in the interlayer space preserves its structure after dehydration, whereas some structural changes were observed for lysozyme adsorbed on the particle surface.
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Sébastien Balme, Régis Guégan, Jean-Marc Janot, Maguy Jaber, Mathilde Lepoitevin, et al.. Structure, Orientation and Stability of Lysozyme Confined in layered Materials. The Royal Society of Chemistry, 2013, 9 (11), pp.3188-3196. ⟨10.1039/C3SM27880H⟩. ⟨insu-00779421v2⟩

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