Abstract
In recent years, much attention has focused on incorporating biological and bio-inspired nanomaterials into various applications that range from functionalising surfaces and enhancing biomolecule binding properties, to coating drugs for improved bioavailability and delivery. Hydrophobin proteins, which can spontaneously assemble into amphipathic layers at hydrophobic:hydrophilic interfaces, are exciting candidates for use as nanomaterials. These unique proteins, which are only expressed by filamentous fungi, have been the focus of increasing interest from the biotechnology industry, as evidenced by the sharply growing number of hydrophobin-associated publications and patents. Here, we explore the contribution of different hydrophobins to supporting fungal growth and development. We describe the key structural elements of hydrophobins and the molecular characteristics that underlie self-assembly of these proteins at interfaces. We outline the multiple roles that hydrophobins can play in supporting aerial growth of filamentous structures, facilitating spore dispersal and preventing an immune response in the infected host. The growing understanding of the hydrophobin protein structure and self-assembly process highlights the potential for hydrophobin proteins to be engineered for use in a variety of novel applications that require biocompatible coatings.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Wösten HAB, van Wetter MA, Lugones LG, van der Mei HC, Busscher HJ, Wessels JGH (1999) How a fungus escapes the water to grow into the air. Curr Biol 9:85–88. https://doi.org/10.1016/S0960-9822(99)80019-0
Beever RE, Dempsey GP (1978) Function of rodlets on the surface of fungal spores. Nature 272:608–610
Aimanianda V, Bayry J, Bozza S, Kniemeyer O, Perruccio K, Elluru SR, Clavaud C, Paris S, Brakhage AA, Kaveri SV, Romani L, Latgé JP (2009) Surface hydrophobin prevents immune recognition of airborne fungal spores. Nature 460:1117–1121. https://doi.org/10.1038/nature08264
Talbot NJ, Ebbole DJ, Hamer JE (1993) Identification and characterization of MPG1, a gene involved in pathogenicity from the rice blast fungus Magnaporthe grisea. Plant Cell 5:1575–1590. https://doi.org/10.1105/tpc.5.11.1575
Wösten HAB, Schuren FH, Wessels JGH (1994) Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces. EMBO J 13:5848–5854
Hess WM, Sassen MMA, Remsen CC (1966) Surface structures of frozen-etched Penicillium conidiospores. Naturwissenschaften 53:708
Hess WM, Sassen MMA, Remsen CC (1968) Surface characteristics of Penicillium conidia. Mycologia 60:290–303
Dempsey GP, Beever RE (1979) Electron microscopy of the rodlet layer of Neurospora crassa conidia. J Bacteriol 140:1050–1062
Beever RE, Redgwell RJ, Dempsey GP (1979) Purification and chemical characterization of the rodlet layer of Neurospora crassa conidia. J Bacteriol 140:1063–1070
Templeton MD, Greenwood DR, Beever RE (1995) Solubilization of Neurospora crassa rodlet proteins and identification of the predominant protein as the proteolytically processed eas (ccg-2) gene product. Exp Mycol 19:166–169
Wessels JGH (1993) Cell wall growth, protein excretion and morphogenesis in fungi. New Phytol 123:397–413
Wessels JGH, de Vries OMH, Asgeirsdottir SA, Schuren FHJ (1991) Hydrophobin genes involved in formation of aerial hyphae and fruit bodies in Schizophyllum. Plant Cell 3:793–799
Linder MB, Szilvay GR, Nakari-Setälä T, Penttilä ME (2005) Hydrophobins: the protein-amphiphiles of filamentous fungi. FEMS Microbiol Rev 29:877–896. https://doi.org/10.1016/j.femsre.2005.01.004
Yang K, Deng Y, Zhang C, Elasri M (2006) Identification of new members of hydrophobin family using primary structure analysis. BMC Bioinforma 7(Suppl 4):S16. https://doi.org/10.1186/1471-2105-7-S4-S16
Jensen BG, Andersen MR, Pedersen MH, Frisvad JC, Søndergaard I (2010) Hydrophobins from Aspergillus species cannot be clearly divided into two classes. BMC Res Notes 3:344. https://doi.org/10.1186/1756-0500-3-344
Mackay JP, Matthews JM, Winefield RD, Mackay LG, Haverkamp RG, Templeton MD (2001) The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. Structure 9:83–91. https://doi.org/10.1016/S0969-2126(00)00559-1
Wessels JGH, Asgeirsdottir SA, Birkenkamp KU, de Vries OMH, Lugones LG, Scheer JMJ, Schuren FH, Schuurs TA, van Wetter M-A, Wösten HAB (1995) Genetic regulation of emergent growth in Schizophyllum commune. Can J Bot 73(Suppl. 1):S273–S281
Grünbacher A, Throm T, Seidel C, Gutt B, Röhrig J, Strunk T, Vincze P, Walheim S, Schimmel T, Wenzel W, Fischer R (2014) Six hydrophobins are involved in hydrophobin rodlet formation in Aspergillus nidulans and contribute to hydrophobicity of the spore surface. PLoS One 9:e94546. https://doi.org/10.1371/journal.pone.0094546
Lacroix H, Whiteford JR, Spanu PD (2008) Localization of Cladosporium fulvum hydrophobins reveals a role for HCf-6 in adhesion. FEMS Microbiol Lett 286:136–144
Whiteford JR, Spanu PD (2001) The hydrophobin HCf-1 of Cladosporium fulvum is required for efficient water-mediated dispersal of conidia. Fungal Genet Biol 32:159–168. https://doi.org/10.1006/fgbi.2001.1263
Lau G, Hamer JE (1996) Regulatory genes controlling MPG1 expression and pathogenicity in the rice blast fungus Magnaporthe grisea. Plant Cell 8:771–781. https://doi.org/10.1105/tpc.8.5.771
Nakari-Setälä T, Aro N, Ilmén M, Muñoz G, Kalkkinen N, Penttilä M (1997) Differential expression of the vegetative and spore-bound hydrophobins of Trichoderma reesei--cloning and characterization of the hfb2 gene. Eur J Biochem 248:415–423
Arpaia G, Loros JJ, Dunlap JC, Morelli G, Macino G (1993) The interplay of light and circadian clock: independent dual regulation of clock-controlled gene ccg-2 (eas). Plant Physiol 102:1299–1305
Sokolovsky VY, Lauter FR, Muller-Rober B, Ricci M, Schmidhauser TJ, Russo VEA (1992) Nitrogen regulation of blue light-inducible genes in Neurospora crassa. J Gen Microbiol 138:2045–2049
Ren Q, Kwan AHY, Sunde M (2013) Two forms and two faces, multiple states and multiple uses: properties and applications of the self-assembling fungal hydrophobins. Biopolymers 100:601–612. https://doi.org/10.1002/bip.22259
Lo VC, Ren Q, Pham CLL, Morris VK, Kwan AHY, Sunde M (2014) Fungal hydrophobin proteins produce self-assembling protein films with diverse structure and chemical stability. Nano 4:827–843. https://doi.org/10.3390/nano4030827
de Vocht ML, Reviakine I, Ulrich WP, Bergsma-Schutter W, Wösten HAB, Vogel H, Brisson A, Wessels JGH, Robillard GT (2002) Self-assembly of the hydrophobin Sc3 proceeds via two structural intermediates. Protein Sci 11:1199–1205
de Vries OMH, Fekkes MP, Wösten HAB, Wessels JGH (1993) Insoluble hydrophobin complexes in the walls of Schizophyllum commune and other filamentous fungi. Arch Microbiol 159:330–335
Wösten HAB, de Vries OMH, Wessels JGH (1993) Interfacial self-assembly of a fungal hydrophobin into a hydrophobic rodlet layer. Plant Cell 5:1567–1574
Butko P, Buford JP, Goodwin JS, Stroud PA, McCormick CL, Cannon CC (2001) Spectroscopic evidence for amyloid-like interfacial self-assembly of hydrophobin Sc3. Biochem Biophys Res Commun 280:212–215. https://doi.org/10.1006/bbrc.2000.4098
Kwan AHY, Winefield RD, Sunde M, Matthews JM, Haverkamp RG, Templeton MD, Mackay JP (2006) Structural basis for rodlet assembly in fungal hydrophobins. Proc Natl Acad Sci USA 103:3621–3626. https://doi.org/10.1073/pnas.0505704103
Kershaw MJ, Wakley G, Talbot NJ (1998) Complementation of the mpg1 mutant phenotype in Magnaporthe grisea reveals functional relationships between fungal hydrophobins. EMBO J 17:3838–3849. https://doi.org/10.1093/emboj/17.14.3838
Hektor HJ, Scholtmeijer K (2005) Hydrophobins: proteins with potential. Curr Opin Biotechnol 16:434–439. https://doi.org/10.1016/j.copbio.2005.05.004
Ren Q, Kwan AHY, Sunde M (2014) Solution structure and interface-driven self-assembly of NC2, a new member of the class II hydrophobin proteins. Proteins 82:990–1003. https://doi.org/10.1002/prot.24473
Szilvay GR, Paananen A, Laurikainen K, Vuorimaa E, Lemmetyinen H, Peltonen J, Linder MB (2007) Self-assembled hydrophobin protein films at the air-water interface: structural analysis and molecular engineering. Biochemistry 46:2345–2354. https://doi.org/10.1021/bi602358h
Hakanpää J, Paananen A, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M, Linder M, Rouvinen J (2004) Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile. J Bio Chem 279:534–539. https://doi.org/10.1074/jbc.M309650200
Hakanpää J, Szilvay GR, Kaljunen H, Maksimainen M, Linder MB, Rouvinen J (2006) Two crystal structures of Trichoderma reesei hydrophobin HFBI—the structure of a protein amphiphile with and without detergent interaction. Protein Sci 15:2129–2140. https://doi.org/10.1110/ps.062326706
Morris VK, Kwan AHY, Sunde M (2013) Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins. J Mol Biol 425:244–256. https://doi.org/10.1016/j.jmb.2012.10.021
Pham CLL, Rey A, Lo VC, Soulès M, Ren Q, Meisl G, Knowles TPJ, Kwan AHY, Sunde M (2016) Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism. Sci Rep 6:25288. https://doi.org/10.1038/srep25288
Sunde M, Kwan AHY, Templeton MD, Beever RE, Mackay JP (2008) Structural analysis of hydrophobins. Micron 39:773–784. https://doi.org/10.1016/j.micron.2007.08.003
Morris VK, Ren Q, Macindoe I, Kwan AHY, Byrne N, Sunde M (2011) Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation. J Biol Chem 286:15955–15963
Askolin S, Linder MB, Scholtmeijer K, Tenkanen M, Penttilä M, de Vocht ML, Wösten HAB (2006) Interaction and comparison of a class I hydrophobin from Schizophyllum commune and class II hydrophobins from Trichoderma reesei. Biomacromolecules 7:1295–1301. https://doi.org/10.1021/bm050676s
van der Vegt W, van der Mei HC, Wösten HAB, Wessels JGH, Busscher HJ (1996) A comparison of the surface activity of the fungal hydrophobin Sc3p with those of other proteins. Biophys Chem 57:253–260
Wang X, Graveland-Bikker JF, de Kruif CG, Robillard GT (2004) Oligomerization of hydrophobin Sc3 in solution: from soluble state to self-assembly. Protein Sci 13:810–821. https://doi.org/10.1110/ps.03367304
de Vocht ML, Scholtmeijer K, van der Vegte EW, de Vries OMH, Sonveaux N, Wösten HAB, Ruysschaert JM, Hadziloannou G, Wessels JGH, Robillard GT (1998) Structural characterization of the hydrophobin Sc3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces. Biophys J 74:2059–2068
Zangi R, de Vocht ML, Robillard GT, Mark AE (2002) Molecular dynamics study of the folding of hydrophobin Sc3 at a hydrophilic/hydrophobic interface. Biophys J 83:112–124. https://doi.org/10.1016/S0006-3495(02)75153-9
Kwan AHY, Macindoe I, Vukasin PV, Morris VK, Kass I, Gupte R, Mark A, Templeton MD, Mackay JP, Sunde M (2008) The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity. J Mol Biol 382:708–720. https://doi.org/10.1016/j.jmb.2008.07.034
Niu B, Gong T, Gao X, Xu H, Qiao M, Li W (2014) The functional role of Cys3-Cys4 loop in hydrophobin HGFI. Amino Acids 46:2615–2625. https://doi.org/10.1007/s00726-014-1805-0
Simone A, Kitchen C, Kwan AHY, Sunde M, Dobson C, Frenkel D (2012) Intrinsic disorder modulates protein self-assembly and aggregation. Proc Natl Acad Sci USA 109:6951–6956
Macindoe I, Kwan AHY, Ren Q, Morris VK, Yang W, Mackay JP, Sunde M (2012) Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS. Proc Natl Acad Sci USA 109:E804–E811. https://doi.org/10.1073/pnas.1114052109
Rambach G, Blum G, Latgé JP, Fontaine T, Heinekamp T, Hagleitner M, Jeckström H, Weigel G, Würtinger P, Pfaller K, Krappmann S, Löffler J, Lass-Flörl C, Speth C (2015) Identification of Aspergillus fumigatus surface components that mediate interaction of conidia and hyphae with human platelets. J Infect Dis 212:1140–1149. https://doi.org/10.1093/infdis/jiv191
Rohde M, Schwienbacher M, Nikolaus T, Heesemann J, Ebel F (2002) Detection of early phase specific surface appendages during germination of Aspergillus fumigatus conidia. FEMS Microbiol Lett 206:99–105
Dague E, Alsteens D, Latgé JP, Dufrêne YF (2008) High-resolution cell surface dynamics of germinating Aspergillus fumigatus conidia. Biophys J 94:656–660. https://doi.org/10.1529/biophysj.107.116491
Carrion SDJ, Leal SM, Ghannoum MA, Aimanianda V, Latgé JP, Pearlman E (2013) The RodA hydrophobin on Aspergillus fumigatus spores masks dectin-1- and dectin-2-dependent responses and enhances fungal survival in vivo. J Immunol 191:2581–2588. https://doi.org/10.4049/jimmunol.1300748
Loures FV, Röhm M, Lee CK, Santos E, Wang JP, Specht CA, Calich VLG, Urban CF, Levitz SM (2015) Recognition of Aspergillus fumigatus hyphae by human plasmacytoid dendritic cells is mediated by dectin-2 and results in formation of extracellular traps. PLoS Pathog 11:e1004643. https://doi.org/10.1371/journal.ppat.1004643
Steele C, Rapaka RR, Metz A, Pop SM, Williams DL, Gordon S, Kolls JK, Brown GD (2005) The beta-glucan receptor dectin-1 recognizes specific morphologies of Aspergillus fumigatus. PLoS Pathog 1:e42. https://doi.org/10.1371/journal.ppat.0010042
Khan NS, Kasperkovitz PV, Timmons AK, Mansour MK, Tam JM, Seward MW, Reedy JL, Puranam S, Feliu M, Vyas JM (2016) Dectin-1 controls TLR9 trafficking to phagosomes containing β-1,3 glucan. J Immunol 196:2249–2261. https://doi.org/10.4049/jimmunol.1401545
Paris S, Debeaupuis JP, Crameri R, Carey M, Charlès F, Prévost MC, Schmitt C, Philippe B, Latgé JP (2003) Conidial hydrophobins of Aspergillus fumigatus. Appl Environ Microbiol 69:1581–1588
Beauvais A, Schmidt C, Guadagnini S, Roux P, Perret E, Henry C, Paris S, Mallet A, Prévost MC, Latgé JP (2007) An extracellular matrix glues together the aerial-grown hyphae of Aspergillus fumigatus. Cell Microbiol 9:1588–1600. https://doi.org/10.1111/j.1462-5822.2007.00895.x
Bruns S, Seidler M, Albrecht D, Salvenmoser S, Remme N, Hertweck C, Brakhage AA, Kniemeyer O, Müller FMC (2010) Functional genomic profiling of Aspergillus fumigatus biofilm reveals enhanced production of the mycotoxin gliotoxin. Proteomics 10:3097–3107. https://doi.org/10.1002/pmic.201000129
Gibbons JG, Beauvais A, Beau R, McGary KL, Latgé JP, Rokas A (2012) Global transcriptome changes underlying colony growth in the opportunistic human pathogen Aspergillus fumigatus. Eukaryot Cell 11:68–78. https://doi.org/10.1128/EC.05102-11
Skamnioti P, Gurr SJ (2007) Magnaporthe grisea cutinase2 mediates appressorium differentiation and host penetration and is required for full virulence. Plant Cell 19:2674–2689. https://doi.org/10.1105/tpc.107.051219
Matsumura H, Reich S, Ito A, Saitoh H, Kamoun S, Winter P, Kahl G, Reuter M, Kruger DH, Terauchi R (2003) Gene expression analysis of plant host-pathogen interactions by SuperSAGE. Proc Natl Acad Sci USA 100:15718–15723. https://doi.org/10.1073/pnas.2536670100
Talbot NJ, Kershaw MJ, Wakley GE, De Vries OMH, Wessels JGH, Hamer JE (1996) MPG1 encodes a fungal hydrophobin involved in surface interactions during infection-related development of Magnaporthe grisea. Plant Cell 8:985–999. https://doi.org/10.1105/tpc.8.6.985
Inoue K, Kitaoka H, Park P, Ikeda K (2015) Novel aspects of hydrophobins in wheat isolate of Magnaporthe oryzae: Mpg1, but not Mhp1, is essential for adhesion and pathogenicity. J Gen Plant Pathol 82:18–28. https://doi.org/10.1007/s10327-015-0632-9
Khalesi M, Deckers SM, Gebruers K, Vissers L, Verachtert H, Derdelinckx G (2012) Hydrophobins: exceptional proteins for many applicaitons in brewery environment and other bio-industries. Cerevisia 37:3–9
Wösten HAB, Scholtmeijer K (2015) Applications of hydrophobins: current state and perspectives. Appl Microbiol Biotechnol 99:1587–1597. https://doi.org/10.1007/s00253-014-6319-x
Wang Z, Lienemann M, Qiau M, Linder MB (2010) Mechanisms of protein adhesion on surface films of hydrophobin. Langmuir 26:8491–8496. https://doi.org/10.1021/la101240e
Longobardi S, Gravagnuolo AM, Funari R, Della Ventura B, Pane F, Galano E, Amoresano A, Marino G, Giardina P (2015) A simple MALDI plate functionalization by Vmh2 hydrophobin for serial multi-enzymatic protein digestions. Anal Bioanal Chem 407:487–496. https://doi.org/10.1007/s00216-014-8309-3
Gravagnuolo AM, Morales-Narváez E, Matos CRS, Longobardi S, Giardina P, Merkoçi A (2015) On-the-spot immobilization of quantum dots, graphene oxide, and proteins via Hydrophobins. Adv Funct Mater 25(38):6084–6092. https://doi.org/10.1002/adfm.201502837
Sapsford KE, Medintz IL, Golden JP, Deschamps JR, Uyeda HT, Mattoussi H (2004) Surface-immobilized self-assembled protein-based quantum dot Nanoassemblies. Langmuir 20(18):7720–7728. https://doi.org/10.1021/la049263n
Haddada MB, Blanchard J, Casale S, Krafft J-M, Vallée A, Méthivier C, Boujday S (2013) Optimizing the immobilization of gold nanoparticles on functionalized silicon surfaces: amine- vs thiol-terminated silane. Gold Bull 46(4):335–341. https://doi.org/10.1007/s13404-013-0120-y
Alves NJ, Kiziltepe T, Bilgicer B (2012) Oriented surface immobilization of antibodies at the conserved nucleotide binding site for enhanced antigen detection. Langmuir 28(25):9640–9648. https://doi.org/10.1021/la301887s
Zhao ZX, Wang HC, Qin X, Wang XS, Qiao MQ, Anzai JI, Chen Q (2009) Self-assembled film of hydrophobins on gold surfaces and its application to electrochemical biosensing. Colloids Surf B Biointerfaces 71:102–106. https://doi.org/10.1016/j.colsurfb.2009.01.011
Wang X, Wang H, Huang Y, Zhao Z, Qin X, Wang Y, Miao Z, Chen Q, Qiao M (2010) Noncovalently functionalized multi-wall carbon nanotubes in aqueous solution using the hydrophobin HFBI and their electroanalytical application. Biosens Bioelectron 26:1104–1108. https://doi.org/10.1016/j.bios.2010.08.024
Rea I, Giardina P, Longobardi S, Porro F, Casuscelli V, Rendina I, De Stefano L (2012) Hydrophobin Vmh2-glucose complexes self-assemble in nanometric biofilms. J R Soc Interface 9:2450–2456. https://doi.org/10.1098/rsif.2012.0217
Politi J, De Stefano L, Rea I, Gravagnuolo A, Giardina P, Methivier C, Casale S, Spadavecchia J (2016) One-pot synthesis of a gold nanoparticle-Vmh2 hydrophobin nanobiocomplex for glucose monitoring. Nanotechnology 27:195701. https://doi.org/10.1088/0957-4484/27/19/195701
Bilewicz R, Witomski J, Van der Heyden A, Tagu D, Palin B, Rogalska E (2001) Modification of electrodes with self-assembled Hydrophobin layers. J Phys Chem B 105(40):9772–9777. https://doi.org/10.1021/jp0113782
Opwis K, Gutmann JS (2011) Surface modification of textile materials with hydrophobins. Text Res J 81:1594–1602
Popescu AC, Stan GE, Duta L, Dorcioman G, Iordache O, Dumitrescu I, Pasuk I, Mihailescu IN (2013) Influence of a hydrophobin underlayer on the structuring and antimicrobial properties of ZnO films. J Mater Sci 48:8329–8336
Lee JH, Khang G, Lee JW, Lee HB (1998) Interaction of different types of cells on polymer surfaces with wettability gradient. J Colloid Interf Sci 205:323–330. https://doi.org/10.1006/jcis.1998.5688
Janssen MI, van Leeuwen MBM, Scholtmeijer K, van Kooten TG, Dijkhuizen L, Wösten HAB (2002) Coating with genetic engineered hydrophobin promotes growth of fibroblasts on a hydrophobic solid. Biomaterials 23:4847–4854
Boeuf S, Throm T, Gutt B, Strunk T, Hoffmann M, Seebach E, Mühlberg L, Brocher J, Gotterbarm T, Wenzel W, Fischer R, Richter W (2012) Engineering hydrophobin DewA to generate surfaces that enhance adhesion of human but not bacterial cells. Acta Biomater 8:1037–1047. https://doi.org/10.1016/j.actbio.2011.11.022
Weickert U, Wiesend F, Subkowski T, Eickhoff A, Reiss G (2011) Optimizing biliary stent patency by coating with hydrophobin alone or hydrophobin and antibiotics or heparin: an in vitro proof of principle study. Adv Med Sci 56:138–144. https://doi.org/10.2478/v10039-011-0026-y
Stanimirova RD, Gurkov TD, Kralchevsky PA, Balashev KT, Stoyanov SD, Pelan EG (2013) Surface pressure and elasticity of hydrophobin HFBII layers on the air-water interface: rheology versus structure detected by AFM imaging. Langmuir 29:6053–6067. https://doi.org/10.1021/la4005104
Deckers SM, Venken T, Khalesi M, Gebruers K, Baggerman G, Lorgouilloux Y, Shokribousjein Z, Ilberg V, Schönberger C, Titze J, Verachtert H, Michiels C, Neven H, Delcour J, Martens J, Derdelinckx G, de Maeyer M (2012) Combined modeling and biophysical characterisation of CO2 interaction with class II hydrophobins: new insight into the mechanism underpinning primary gushing. J Am Soc Brew Chem 70:249–256
Cox AR, Aldred DL, Russell AB (2009) Exceptional stability of food foams using class II hydrophobin HFBII. Food Hydrocoll 23:366–376. https://doi.org/10.1016/j.foodhyd.2008 .03.001
Tchuenbou-Magaia FL, Norton IT, Cox PW (2009) Hydrophobins stabilised air-filled emulsions for the food industry. Food Hydrocoll 23:1877–1885. https://doi.org/10.1016/j.foodhyd.2009.03.005
Green A, Littlejohn K, Hooley P, Cox P (2013) Formation and stability of food foams and aerated emulsions: hydrophobins as novel functional ingredients. Curr Opin Colloid Interface Sci 18(4):292–301
Loftsson T, Brewster ME (2010) Pharmaceutical applications of cyclodextrins: basic science and product development. J Pharm Pharmacol 62:1607–1621. https://doi.org/10.1111/j.2042-7158.2010.01030.x
Haas Jimoh Akanbi M, Post E, Meter-Arkema A, Rink R, Robillard GT, Wang X, Wösten HAB, Scholtmeijer K (2010) Use of hydrophobins in formulation of water insoluble drugs for oral administration. Colloids Surf B Biointerfaces 75:526–531. https://doi.org/10.1016/j.colsurfb.2009.09.030
Fang G, Tang B, Liu Z, Gou J, Zhang Y, Xu H, Tang X (2014) Novel hydrophobin-coated docetaxel nanoparticles for intravenous delivery: in vitro characteristics and in vivo performance. Eur J Pharm Sci 60:1–9. https://doi.org/10.1016/j.ejps.2014.04.016
Valo HK, Laaksonen PH, Peltonen LJ, Linder MB, Hirvonen JT, Laaksonen TJ (2010) Multifunctional hydrophobin: toward functional coatings for drug nanoparticles. ACS Nano 4:1750–1758. https://doi.org/10.1021/nn9017558
Yang W, Ren Q, Wu YN, Morris VK, Rey AA, Braet F, Kwan AHY, Sunde M (2013) Surface functionalization of carbon nanomaterials by self-assembling hydrophobin proteins. Biopolymers 99:84–94. https://doi.org/10.1002/bip.22146
Sarparanta M, Bimbo LM, Rytkönen J, Mäkilä E, Laaksonen TJ, Laaksonen P, Nyman M, Salonen J, Linder MB, Hirvonen J, Santos HA, Airaksinen AJ (2012) Intravenous delivery of hydrophobin-functionalized porous silicon nanoparticles: stability, plasma protein adsorption and biodistribution. Mol Pharm 9:654–663. https://doi.org/10.1021/mp200611d
Acknowledgements
The authors gratefully acknowledge the support of the Australian Research Council in the form of Discovery Grants DP120100756 and DP150104227 to MS, which have supported research into the structure and properties of hydrophobin proteins. VL and JL are supported by Australian Postgraduate Awards. We also thank Dr. Ann Kwan for her contributions to this work.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Lo, V., I-Chun Lai, J., Sunde, M. (2019). Fungal Hydrophobins and Their Self-Assembly into Functional Nanomaterials. In: Perrett, S., Buell, A., Knowles, T. (eds) Biological and Bio-inspired Nanomaterials. Advances in Experimental Medicine and Biology, vol 1174. Springer, Singapore. https://doi.org/10.1007/978-981-13-9791-2_5
Download citation
DOI: https://doi.org/10.1007/978-981-13-9791-2_5
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-13-9790-5
Online ISBN: 978-981-13-9791-2
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)