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• W2000507107 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." @default.
• W2000507107 created "2016-06-24" @default.
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• W2000507107 date "2006-05-28" @default.
• W2000507107 modified "2023-10-13" @default.
• W2000507107 title "Analytical Investigation of the Interactions between SC3 Hydrophobin and Lipid Layers: Elaborating of Nanostructured Matrixes for Immobilizing Redox Systems" @default.
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• W2000507107 doi "https://doi.org/10.1021/ac0602064" @default.
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