ArticleBiophysical journal2005
The SC3 hydrophobin self-assembles into a membrane with distinct mass transfer properties.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Integrative workflows for the characterization of hydrophobin and cerato-platanin in the marine fungus Paradendryphiella salina.Archives of microbiology · 2024Article
- "You Are What You Eat": How Fungal Adaptation Can Be Leveraged toward Myco-Material Properties.Global challenges (Hoboken, NJ) · 2024Article
- The Role of thePathogens (Basel, Switzerland) · 2023Article
- Versatile biomimetic medical device surface: hydrophobin coated, nitric oxide-releasing polymer for antimicrobial and hemocompatible applications.Biomaterials science · 2019Article
- Fungal hydrophobins render stones impermeable for water but keep them permeable for vapor.Scientific reports · 2019Article
- Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles.ChemistryOpen · 2018Article
- Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.Scientific reports · 2017Article
- Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins.BMC biotechnology · 2013Article
- Hydrophobins--unique fungal proteins.PLoS pathogens · 2012Article
- Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation.The Journal of biological chemistry · 2011Article
- Creating Surface Properties Using a Palette of Hydrophobins.Materials (Basel, Switzerland) · 2010Review
- Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana.Plant physiology · 2010Article
- Assembly of the fungal SC3 hydrophobin into functional amyloid fibrils depends on its concentration and is promoted by cell wall polysaccharides.The Journal of biological chemistry · 2009Article
- Interactions of hydrophobin proteins in solution studied by small-angle X-ray scattering.Biophysical journal · 2008Article
- Structural basis for rodlet assembly in fungal hydrophobins.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrophobins are a class of small proteins that fulfill a wide spectrum of functions in fungal growth and development. They do so by self-assembling into an amphipathic membrane at hydrophilic-hydrophobic interfaces. The SC3 hydrophobin of Schizophyllum commune is the best-studied hydrophobin. It assembles at the air-water interface into a membrane consisting of functional amyloid fibrils that are called rodlets. Here we examine the dynamics of SC3 assembly at an oil-water and air-water interface and the permeability characteristics of the assembled layer. Hydrophobin assembled at an oil-water interface is a dynamic system capable of emulsifying oil. It accepts soluble-state SC3 oligomers from water in a unidirectional process and sloughs off SC3 vesicles back into the water phase enclosing a portion of the oil phase in their hydrophobic interior. The assembled layer is impermeable to solutes >200 Da from either the water phase or the oil phase; however, due to the emulsification process, oil and the hydrophobic marker molecules in the oil phase can be transferred into the water phase, thus giving the impression that the assembled layer is permeable to the marker molecules. By contrast, the layer assembled at an air-water interface is permeable to water vapor from either the hydrophobic or hydrophilic side.
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