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Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins

Class I hydrophobins produced from fungi are amongst the first proteins recognized as functional amyloids. They are amphiphilic proteins involved in the formation of aerial structures such as spores or fruiting bodies. They form chemically robust layers which can only be dissolved in strong acids. T...

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Detalles Bibliográficos
Autores principales: Piscitelli, Alessandra, Cicatiello, Paola, Gravagnuolo, Alfredo Maria, Sorrentino, Ilaria, Pezzella, Cinzia, Giardina, Paola
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618226/
https://www.ncbi.nlm.nih.gov/pubmed/28672843
http://dx.doi.org/10.3390/biom7030045
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author Piscitelli, Alessandra
Cicatiello, Paola
Gravagnuolo, Alfredo Maria
Sorrentino, Ilaria
Pezzella, Cinzia
Giardina, Paola
author_facet Piscitelli, Alessandra
Cicatiello, Paola
Gravagnuolo, Alfredo Maria
Sorrentino, Ilaria
Pezzella, Cinzia
Giardina, Paola
author_sort Piscitelli, Alessandra
collection PubMed
description Class I hydrophobins produced from fungi are amongst the first proteins recognized as functional amyloids. They are amphiphilic proteins involved in the formation of aerial structures such as spores or fruiting bodies. They form chemically robust layers which can only be dissolved in strong acids. These layers adhere to different surfaces, changing their wettability, and allow the binding of other proteins. Herein, the modification of diverse types of surfaces with Class I hydrophobins is reported, highlighting the applications of the coated surfaces. Indeed, these coatings can be exploited in several fields, spanning from biomedical to industrial applications, which include biosensing and textile manufacturing.
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spelling pubmed-56182262017-09-29 Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins Piscitelli, Alessandra Cicatiello, Paola Gravagnuolo, Alfredo Maria Sorrentino, Ilaria Pezzella, Cinzia Giardina, Paola Biomolecules Review Class I hydrophobins produced from fungi are amongst the first proteins recognized as functional amyloids. They are amphiphilic proteins involved in the formation of aerial structures such as spores or fruiting bodies. They form chemically robust layers which can only be dissolved in strong acids. These layers adhere to different surfaces, changing their wettability, and allow the binding of other proteins. Herein, the modification of diverse types of surfaces with Class I hydrophobins is reported, highlighting the applications of the coated surfaces. Indeed, these coatings can be exploited in several fields, spanning from biomedical to industrial applications, which include biosensing and textile manufacturing. MDPI 2017-06-26 /pmc/articles/PMC5618226/ /pubmed/28672843 http://dx.doi.org/10.3390/biom7030045 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Piscitelli, Alessandra
Cicatiello, Paola
Gravagnuolo, Alfredo Maria
Sorrentino, Ilaria
Pezzella, Cinzia
Giardina, Paola
Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title_full Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title_fullStr Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title_full_unstemmed Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title_short Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins
title_sort applications of functional amyloids from fungi: surface modification by class i hydrophobins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618226/
https://www.ncbi.nlm.nih.gov/pubmed/28672843
http://dx.doi.org/10.3390/biom7030045
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