Next Article in Journal
A Novel Method to Determine the Thermal Conductivity of Interfacial Layers Surrounding the Nanoparticles of a Nanofluid
Next Article in Special Issue
In Situ Self Assembly of Nanocomposites: Competition of Chaotic Advection and Interfacial Effects as Observed by X-Ray Diffreaction
Previous Article in Journal
Encapsulation of Anti-Tuberculosis Drugs within Mesoporous Silica and Intracellular Antibacterial Activities
Previous Article in Special Issue
Self-Assembly in Biosilicification and Biotemplated Silica Materials
Article

Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability

1
Discipline of Pharmacology, School of Medical Sciences, The University of Sydney, Sydney NSW 2006, Australia
2
School of Molecular Bioscience, The University of Sydney, Sydney NSW 2006, Australia
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Nanomaterials 2014, 4(3), 827-843; https://doi.org/10.3390/nano4030827
Received: 23 June 2014 / Revised: 22 August 2014 / Accepted: 5 September 2014 / Published: 17 September 2014
(This article belongs to the Special Issue Self-Assembled Nanomaterials)
Hydrophobins are small proteins secreted by fungi and which spontaneously assemble into amphipathic layers at hydrophilic-hydrophobic interfaces. We have examined the self-assembly of the Class I hydrophobins EAS∆15 and DewA, the Class II hydrophobin NC2 and an engineered chimeric hydrophobin. These Class I hydrophobins form layers composed of laterally associated fibrils with an underlying amyloid structure. These two Class I hydrophobins, despite showing significant conformational differences in solution, self-assemble to form fibrillar layers with very similar structures and require a hydrophilic-hydrophobic interface to trigger self-assembly. Addition of additives that influence surface tension can be used to manipulate the fine structure of the protein films. The Class II hydrophobin NC2 forms a mesh-like protein network and the engineered chimeric hydrophobin displays two multimeric forms, depending on assembly conditions. When formed on a graphite surface, the fibrillar EAS∆15 layers are resistant to alcohol, acid and basic washes. In contrast, the NC2 Class II monolayers are dissociated by alcohol treatment but are relatively stable towards acid and base washes. The engineered chimeric Class I/II hydrophobin shows increased stability towards alcohol and acid and base washes. Self-assembled hydrophobin films may have extensive applications in biotechnology where biocompatible; amphipathic coatings facilitate the functionalization of nanomaterials. View Full-Text
Keywords: hydrophobin; protein; film; amphipathic; self-assembly hydrophobin; protein; film; amphipathic; self-assembly
Show Figures

Graphical abstract

MDPI and ACS Style

Lo, V.C.; Ren, Q.; Pham, C.L.L.; Morris, V.K.; Kwan, A.H.; Sunde, M. Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability. Nanomaterials 2014, 4, 827-843. https://doi.org/10.3390/nano4030827

AMA Style

Lo VC, Ren Q, Pham CLL, Morris VK, Kwan AH, Sunde M. Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability. Nanomaterials. 2014; 4(3):827-843. https://doi.org/10.3390/nano4030827

Chicago/Turabian Style

Lo, Victor C., Qin Ren, Chi L.L. Pham, Vanessa K. Morris, Ann H. Kwan, and Margaret Sunde. 2014. "Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability" Nanomaterials 4, no. 3: 827-843. https://doi.org/10.3390/nano4030827

Find Other Styles

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Back to TopTop