title: Analytical investigation of the interactions between SC3 hydrophobin and lipid layers: elaborating of nanostructured matrixes for immobilizing redox systems.
abstract: Hydrophobins are highly tensioactive fungal proteins with a pronounced affinity for interfaces and a propensity for self-assembly. Recently, these proteins were shown to be useful in retaining different molecules on solid surfaces. This finding offers a possibility for developing new functional materials, while creating the necessity of further research at a deeper mechanistic level. In this work, the mechanisms governing the surface phenomena were studied using native Schizophyllum commune hydrophobin (SC3) and lipid mono- and bilayers; the soft matter systems were used to get a handle on the interactive protein/interface effects at a molecular level. The results obtained indicated that the SC3/lipid membrane interactions were adjusted by protein conformational adaptation, allowing its incorporation into lipid matrixes; the incorporation of a chelating SC3 hydrophobin (PFA-SC3) in a monoolein cubic phase yielded a biomimetic, cell-like system of Cu(II) cation immobilization. This system, which is suitable for modifying electrode surface and monitoring the Cu(II)/Cu(0) redox process, may be of practical interest in switching and sensing.
authors.affiliation: Groupe d'Etude des Vecteurs Supramoléculaires du Médicament UMR 7565 CNRS/Université Henri Poincaré Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, France.
authors.forename: Yohann
authors.initials: Y
authors.lastname: Corvis
authors.forename: Gerald
authors.initials: G
authors.lastname: Brezesinski
authors.forename: Rick
authors.initials: R
authors.lastname: Rink
authors.forename: Alain
authors.initials: A
authors.lastname: Walcarius
authors.forename: Angéline
authors.initials: A
authors.lastname: Van der Heyden
authors.forename: Fabrice
authors.initials: F
authors.lastname: Mutelet
authors.forename: Ewa
authors.initials: E
authors.lastname: Rogalska
mesh_terms: D005656:Fungal Proteins / Q000032:analysis* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010084:Oxidation-Reduction; D011485:Protein Binding; D012567:Schizophyllum; D014732:Vibration; D014961:X-Ray Diffraction
chemical_list: D005656:Fungal Proteins