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

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.

Domains: Continental interfaces, environment; Global Changes

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⟩