Spontaneous Surface Self-Assembly in Protein鈥揝urfactant Mixtures: Interactions between Hydrophobin and Ethoxylated Polysorbate Surfactants

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• 作者：Ian M. Tucker ; Jordan T. Petkov ; Jeffrey Penfold ; Robert K. Thomas ; Peixun Li ; Andrew R. Cox ; Nick Hedges ; John R. P. Webster
• 刊名：Journal of Physical Chemistry B
• 出版年：2014
• 出版时间：May 8, 2014
• 年：2014
• 卷：118
• 期：18
• 页码：4867-4875
• 全文大小：411K
• 年卷期：v.118,no.18(May 8, 2014)
• ISSN：1520-5207

文摘

The synergistic interactions between certain ethoxylated polysorbate nonionic surfactants and the protein hydrophobin result in spontaneous self-assembly at the air鈥搘ater interface to form layered surface structures. The surface structures are characterized using neutron reflectivity. The formation of the layered surface structures is promoted by the hydrophobic interaction between the polysorbate alkyl chain and the hydrophobic patch on the surface of the globular hydrophobin and the interaction between the ethoxylated sorbitan headgroup and hydrophilic regions of the protein. The range of the ethoxylated polysorbate concentrations over which the surface ordering occurs is a maximum for the more hydrophobic surfactant polyoxyethylene(8) sorbitan monostearate. The structures at the air鈥搘ater interface are accompanied by a profound change in the wetting properties of the solution on hydrophobic substrates. In the absence of the polysorbate surfactant, hydrophobin wets a hydrophobic surface, whereas the hydrophobin/ethoxylated polysorbate mixtures where multilayer formation occurs result in a significant dewetting of hydrophobic surfaces. The spontaneous surface self-assembly for hydrophobin/ethoxylated polysorbate surfactant mixtures and the changes in surface wetting properties provide a different insight into protein鈥搒urfactant interactions and potential for manipulating surface and interfacial properties and protein surface behavior.