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

The synergistic interactions between certain ethoxylated polysorbate nonionic surfactants and the protein hydrophobin result in spontaneous self-assembly at the air–water interface to form layered surface structures. The surface structures are characterized using neutron reflectivity. The formation...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2014-05, Vol.118 (18), p.4867-4875
Main Authors: Tucker, Ian M, Petkov, Jordan T, Penfold, Jeffrey, Thomas, Robert K, Li, Peixun, Cox, Andrew R, Hedges, Nick, Webster, John R. P
Format: Article
Language:English
Subjects:
Adsorption
Formations
Fungal Proteins - chemistry
Fungi - chemistry
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Multilayers
Polysorbates - chemistry
Proteins
Self assembly
Spontaneous
Surface Properties
Surface structure
Surface-Active Agents - chemistry
Surfactants
Water - chemistry
Wettability
Wetting
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Summary:The synergistic interactions between certain ethoxylated polysorbate nonionic surfactants and the protein hydrophobin result in spontaneous self-assembly at the air–water 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–water 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–surfactant interactions and potential for manipulating surface and interfacial properties and protein surface behavior.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp502413p