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Surface-Induced Hydrophobin Assemblies with Versatile Properties and Distinct Underlying Structures
Rezwan Siddiquee1, Victor Lo2, Caitlin L Johnston2
1School of Life and Environmental Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.
Hydrophobins (proteins) can coat various materials, altering their properties. Surprisingly, not all functional amyloid forms are detergent-resistant, opening new applications for these versatile proteins.
Area of Science:
- Protein science
- Materials science
- Nanotechnology
Background:
- Hydrophobins are proteins known for self-assembly into amphipathic coatings.
- These coatings can reverse surface wettability.
- Class I hydrophobins, like EASΔ15 and DewY, show potential in various applications.
Purpose of the Study:
- To demonstrate the versatility of Class I hydrophobins (EASΔ15 and DewY) in nanosuspension and coating applications.
- To investigate how hydrophobins interact with and modify different substrates.
- To explore the structural properties and stability of hydrophobin coatings.
Main Methods:
- Coating or emulsifying substrates such as oil, hydrophobic drugs, and nanodiamonds with hydrophobins.
- Assessing the solution and surface behavior of modified substrates.
- Testing the resistance of hydrophobin coatings to hot detergent treatment.
Main Results:
- Hydrophobins successfully coated and emulsified diverse substrates, altering their properties.
- Only a subset of hydrophobin coatings exhibited resistance to hot detergent treatment.
- Substrate surface properties were found to influence hydrophobin molecular structures and physiochemical properties.
Conclusions:
- Amyloid formation is not essential for Class I hydrophobins to be functional in diverse applications.
- Findings suggest potential for using hydrophobins in applications requiring varied chemical and physical properties.
- Environmental cues may lead Class I hydrophobins to adopt alternative structures, impacting their properties.
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