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 CuII cation immobilization. This system, which is suitable for modifying electrode surface and monitoring the CuII/Cu0 redox process, may be of practical interest in switching and sensing.
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https://hal.univ-lorraine.fr/hal-01941949
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Submitted on : Sunday, December 2, 2018 - 7:23:27 PM
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Yohann Corvis, Gerald Brezesinski, Rick Rink, Alain Walcarius, Angéline van der Heyden, et al.. Analytical Investigation of the Interactions between SC3 Hydrophobin and Lipid Layers: Elaborating of Nanostructured Matrixes for Immobilizing Redox Systems. Analytical Chemistry, American Chemical Society, 2006, 78 (14), pp.4850-4864. ⟨10.1021/ac0602064⟩. ⟨hal-01941949⟩

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