Literature DB >> 15950452

Hydrophobins: proteins with potential.

Harm J Hektor1, Karin Scholtmeijer.   

Abstract

Hydrophobins are self-assembling proteins of fungal origin. Their ability to self-assemble into an amphipathic membrane is of interest for many different applications, ranging from medical and technical coatings to the production of proteinaceous glue and cosmetics. Assembled hydrophobins can modify surface characteristics, thus controling the binding properties of the surface; for example, enzymes can be actively and non-covalently immobilized on electrode surfaces and medical coatings can be improved for biocompatibility. Over the past few years research on hydrophobins has contributed to a better understanding of the self-assembly process and is generating more handles to control and manipulate the process. This knowledge could have an immediate effect on production levels, which are not yet adequate, and provide the boost needed for hydrophobins to reach their full potential.

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Year:  2005        PMID: 15950452     DOI: 10.1016/j.copbio.2005.05.004

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  27 in total

1.  Expression and purification of a functionally active class I fungal hydrophobin from the entomopathogenic fungus Beauveria bassiana in E. coli.

Authors:  Brett H Kirkland; Nemat O Keyhani
Journal:  J Ind Microbiol Biotechnol       Date:  2010-07-17       Impact factor: 3.346

2.  Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins.

Authors:  Wendel Wohlleben; Thomas Subkowski; Claus Bollschweiler; Bernhard von Vacano; Yaqian Liu; Wolfgang Schrepp; Ulf Baus
Journal:  Eur Biophys J       Date:  2009-03-17       Impact factor: 1.733

3.  Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus.

Authors:  L De Stefano; I Rea; E De Tommasi; I Rendina; L Rotiroti; M Giocondo; S Longobardi; A Armenante; P Giardina
Journal:  Eur Phys J E Soft Matter       Date:  2009-09-18       Impact factor: 1.890

4.  Interfacial self-assembly of a bacterial hydrophobin.

Authors:  Keith M Bromley; Ryan J Morris; Laura Hobley; Giovanni Brandani; Rachel M C Gillespie; Matthew McCluskey; Ulrich Zachariae; Davide Marenduzzo; Nicola R Stanley-Wall; Cait E MacPhee
Journal:  Proc Natl Acad Sci U S A       Date:  2015-04-13       Impact factor: 11.205

Review 5.  Recent Advances in Fungal Hydrophobin Towards Using in Industry.

Authors:  Mohammadreza Khalesi; Kurt Gebruers; Guy Derdelinckx
Journal:  Protein J       Date:  2015-08       Impact factor: 2.371

6.  Two crystal structures of Trichoderma reesei hydrophobin HFBI--the structure of a protein amphiphile with and without detergent interaction.

Authors:  Johanna Hakanpää; Géza R Szilvay; Heidi Kaljunen; Mirko Maksimainen; Markus Linder; Juha Rouvinen
Journal:  Protein Sci       Date:  2006-08-01       Impact factor: 6.725

7.  Kinetics of Surface-Driven Self-Assembly and Fatigue-Induced Disassembly of a Virus-Based Nanocoating.

Authors:  Alejandro Valbuena; Mauricio G Mateu
Journal:  Biophys J       Date:  2017-02-28       Impact factor: 4.033

8.  Surface hydrophobin prevents immune recognition of airborne fungal spores.

Authors:  Vishukumar Aimanianda; Jagadeesh Bayry; Silvia Bozza; Olaf Kniemeyer; Katia Perruccio; Sri Ramulu Elluru; Cécile Clavaud; Sophie Paris; Axel A Brakhage; Srini V Kaveri; Luigina Romani; Jean-Paul Latgé
Journal:  Nature       Date:  2009-08-27       Impact factor: 49.962

9.  Hydrophobin Vmh2-glucose complexes self-assemble in nanometric biofilms.

Authors:  Ilaria Rea; Paola Giardina; Sara Longobardi; Fabrizio Porro; Valeria Casuscelli; Ivo Rendina; Luca De Stefano
Journal:  J R Soc Interface       Date:  2012-05-09       Impact factor: 4.118

10.  Novel hydrophobins from Trichoderma define a new hydrophobin subclass: protein properties, evolution, regulation and processing.

Authors:  Verena Seidl-Seiboth; Sabine Gruber; Ugur Sezerman; Torsten Schwecke; Aydin Albayrak; Torsten Neuhof; Hans von Döhren; Scott E Baker; Christian P Kubicek
Journal:  J Mol Evol       Date:  2011-03-22       Impact factor: 2.395

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