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

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          Abstract

          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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          Most cited references59

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          Prions as adaptive conduits of memory and inheritance.

          Changes in protein conformation drive most biological processes, but none have seized the imagination of scientists and the public alike as have the self-replicating conformations of prions. Prions transmit lethal neurodegenerative diseases by means of the food chain. However, self-replicating protein conformations can also constitute molecular memories that transmit genetic information. Here, we showcase definitive evidence for the prion hypothesis and discuss examples in which prion-encoded heritable information has been harnessed during evolution to confer selective advantages. We then describe situations in which prion-enciphered events might have essential roles in long-term memory formation, transcriptional memory and genome-wide expression patterns.
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            Hydrophobins: Proteins that self assemble at interfaces

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              Structural basis for rodlet assembly in fungal hydrophobins.

              Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are formed. There are also significant similarities between these polymers and amyloid-like fibrils. However, structural information on these proteins and the rodlets they form has been elusive. Here, we describe the three-dimensional structure of the monomeric form of the class I hydrophobin EAS. EAS forms a beta-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface. This structure is consistent with its ability to form an amphipathic polymer. By using this structure, together with data from mutagenesis and previous biophysical studies, we have been able to propose a model for the polymeric rodlet structure adopted by these proteins. X-ray fiber diffraction data from EAS rodlets are consistent with our model. Our data provide molecular insight into the nature of hydrophobin rodlet films and extend our understanding of the fibrillar beta-structures that continue to be discovered in the protein world.
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                Author and article information

                Contributors
                Role: Academic Editor
                Role: Academic Editor
                Role: Academic Editor
                Role: Academic Editor
                Journal
                Biomolecules
                Biomolecules
                biomolecules
                Biomolecules
                MDPI
                2218-273X
                26 June 2017
                September 2017
                : 7
                : 3
                : 45
                Affiliations
                [1 ]Department of Chemical Sciences, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Naples, Italy; apiscite@ 123456unina.it (A.P.); paola.cicatiello@ 123456unina.it (P.C.); alfredo.gravagnuolo@ 123456manchester.ac.uk (A.M.G.); ilaria.sorrentino@ 123456unina.it (I.S.); cpezzella@ 123456unina.it (C.P.)
                [2 ]Division of Pharmacy and Optometry, Faculty of Biology, Medicine and Health, The University of Manchester, M13 9PT Manchester, UK
                Author notes
                [* ]Correspondence: giardina@ 123456unina.it ; Tel.: +39-081-674-319
                Author information
                https://orcid.org/0000-0002-3818-6539
                Article
                biomolecules-07-00045
                10.3390/biom7030045
                5618226
                28672843
                74a1c53c-31bb-417b-bc5c-812ef4c314ba
                © 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/).

                History
                : 15 May 2017
                : 22 June 2017
                Categories
                Review

                functionalization,adhesion,biosensors,protein immobilization,biomedical applications,nanomaterials

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