Self-Assembly of Hydrophobin and Hydrophobin/Surfactant Mixtures in Aqueous Solution
Autor: | Jordan T. Petkov, Jeffrey Penfold, Julian Bent, Robert Thomas, X.L. Zhang, Ian M. Tucker, Isabelle Grillo, Andrew Richard Cox |
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Rok vydání: | 2011 |
Předmět: |
Models
Molecular Ammonium bromide Surface Properties Hydrophobin Inorganic chemistry Micelle Fungal Proteins Surface-Active Agents chemistry.chemical_compound Pulmonary surfactant Scattering Small Angle Electrochemistry General Materials Science Sodium dodecyl sulfate Micelles Spectroscopy Aggregation number Aqueous solution Water Surfaces and Interfaces Condensed Matter Physics Solutions Neutron Diffraction chemistry Chemical engineering Adsorption Self-assembly |
Zdroj: | Langmuir. 27:10514-10522 |
ISSN: | 1520-5827 0743-7463 |
DOI: | 10.1021/la2020226 |
Popis: | The self-assembly of the protein hydrophobin, HFBII, and its self-assembly with cationic, anionic, and nonionic surfactants hexadecylterimethyl ammonium bromide, CTAB, sodium dodecyl sulfate, SDS, and hexaethylene monododecyl ether, C(12)E(6), in aqueous solution have been studied by small-angle neutron scattering, SANS. HFBII self-assembles in solution as small globular aggregates, consistent with the formation of trimers or tetramers. Its self-assembly is not substantially affected by the pH or electrolytes. In the presence of CTAB, SDS, or C(12)E(6), HFBII/surfactant complexes are formed. The structure of the HFBII/surfactant complexes has been identified using contrast variation and is in the form of HFBII molecules bound to the outer surface of globular surfactant micelles. The binding of HFBII decreases the surfactant micelle aggregation number for increasing HFBII concentration in solution, and the number of hydrophobin molecules bound/micelle increases. |
Databáze: | OpenAIRE |
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