3 years ago

Self-assembly of two hydrophobins from marine fungi affected by interaction with surfaces

Self-assembly of two hydrophobins from marine fungi affected by interaction with surfaces
Luca De Stefano, Principia Dardano, Paola Giardina, Alfredo M. Gravagnuolo, Paola Cicatiello, Marinella Pirozzi
Hydrophobins are amphiphilic fungal proteins endowed with peculiar characteristics, such as a high surface activity and an interface triggered self-assembly. Several applications of these proteins have been proposed in the food, cosmetics and biomedical fields. Moreover, their use as proteinaceous coatings can be effective for materials and nanomaterials applications. The discovery of novel hydrophobins with diverse properties may be advantageous from both the scientific and industrial points of view. Stressful environmental conditions of fungal growth may induce the production of proteins with peculiar features. Two Class I hydrophobins from fungi isolated from marine environment have been recently purified. Herein, their propensity to aggregate forming nanometric fibrillar structures has been compared, using different techniques, such as circular dichroism, dynamic light scattering and Thioflavin T fluorescence assay. Furthermore, TEM and AFM images indicate that the interaction of these proteins with specific surfaces, are crucial in the formation of amyloid fibrils and in the assembly morphologies. These self-assembling proteins show promising properties as bio-coating for different materials via a green process. Biotechnol. Bioeng. 2017;9999: 1–14. © 2017 Wiley Periodicals, Inc. Two class I hydrophobins, isolated from marine fungi, are stable in ethanol solution and form amyloid aggregates in aqueous buffer solution with different kinetics. They form amyloid fibrils with different morphologies on surfaces with opposite wettability . The hydrophobins aggregates differently graft surfaces and resist to harsh washing.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/bit.26344

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