Two crystal structures of <i>Trichoderma reesei</i> hydrophobin HFBI—The structure of a protein amphiphile with and without detergent interaction

Hakanpää, Johanna; Szilvay, Géza R.; Kaljunen, Heidi; Maksimainen, Mirko M.; Linder, Markus B.; Rouvinen, Juha

doi:10.1110/ps.062326706

Cited by 154 publications

(248 citation statements)

References 47 publications

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“…HFBII features fi ve positively charged amino acids on the exposed hydrophilic side, [ 21,36,37 ] and its isoelectric point (pI) was measured to be 5.8 (see Figure S1 and Table S1 of the Supporting Information). Therefore, the hypothesized interaction between HFBII and F10 was expected to be electrostatic and pH dependent.…”

Section: Resultsmentioning

confidence: 99%

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Gazzera

Corti

Pirrie

et al. 2015

Adv Materials Inter

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thick fi lm to achieve signifi cant durability and, therefore, requires a relatively large amount of fl uoropolymer. Alternative approaches, such as chemical grafting of fl uoropolymers by radical methods through irradiation, [ 6−8 ] plasma, [ 9−12 ] or direct fl uorination with fl uorine gas, [ 1,2,13 ] require only moderate amounts of fl uorinated surface modifi ers but are much more aggressive and, in some cases, potentially hazardous.Other possibilities involve functionalization with fl uorinated molecules/ polymers consisting of specifi c chemical moieties that are able to bind either covalently or noncovalently to the polymer surface. [ 4,5,14,15 ] However, to achieve sufficiently stable bonding, this general strategy requires the presence of reactive hydrophilic sites, typically OH groups, which are not typically observed on the surfaces of apolar, hydrophobic polymers, such as polyolefi ns, and need to be introduced via oxidizing pretreatments that are usually either energy-intensive or not environmentally friendly. [ 16−19 ] Expanding on this strategy, we present an effi cient, rapid, and more environmentally friendly method to perform the fl uorocarbon coating of hydrophobic polymer surfaces. The method is based on the use of hydrophobins, i.e., amphiphilic surface-active proteins, as a nanosized primer layer that adheres to the hydrophobic polymer surface, making the surface hydrophilic and preparing it for the subsequent binding of a fl uoropolymer containing ionic moieties.Hydrophobins are a class of nontoxic, surface-active, and fi lm-forming proteins that are produced by fi lamentous A new and simple method is presented to fl uorinate the surfaces of poorly reactive hydrophobic polymers in a more environmentally friendly way using the protein hydrophobin (HFBII) as a nanosized primer layer. In particular, HFBII, via electrostatic interactions, enables the otherwise ineffi cient binding of a phosphate-terminated perfl uoropolyether onto polystyrene, polypropylene, and low-density polyethylene surfaces. The binding between HFBII and the perfl uoropolyether depends signifi cantly on the environmental pH, reaching the maximum stability at pH 4. Upon treatment, the polymeric surfaces mostly retain their hydrophobic character but also acquire remarkable oil repellency, which is not observed in the absence of the protein primer. The functionalization proceeds rapidly and spontaneously at room temperature in aqueous solutions without requiring energy-intensive procedures, such as plasma or irradiation treatments.

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Section: Resultsmentioning

confidence: 99%

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Gazzera

Corti

Pirrie

et al. 2015

Adv Materials Inter

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“…C6, C2-C5, C3-C4, and C7-C8 (Hakanpää et al 2004(Hakanpää et al , 2006aKershaw et al 2005;Kwan et al 2006Kwan et al , 2008Morris et al 2012;Ren et al 2013a, b;Pille et al 2014). The cysteine residues are important to keep the protein in the soluble state, at least in the case of the class I hydrophobin SC3 from Schizophyllum commune (de .…”

Section: Introductionmentioning

confidence: 99%

“…The 3D structure of the soluble state of the class I hydrophobins EAS (Neurospora crassa), DewA (Aspergillus nidulans), MPG1 (Magnaporthe grisea), and RodA (Aspergillus fumigatus) (Kwan et al 2006;Morris et al 2012Morris et al , 2013Rey et al 2013;Pille et al 2014) and the class II hydrophobins HFBI, HFBII (Trichoderma reesei), and NC2 (N. crassa) (Hakanpää et al 2004(Hakanpää et al , 2006aRen et al 2013b) has been solved. Both types of hydrophobin contain a four-stranded β-barrel core (Fig.…”

Section: Introductionmentioning

confidence: 99%

Applications of hydrophobins: current state and perspectives

Wösten

Scholtmeijer

2015

Appl Microbiol Biotechnol

142

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Hydrophobins are proteins exclusively produced by filamentous fungi. They self-assemble at hydrophilichydrophobic interfaces into an amphipathic film. This protein film renders hydrophobic surfaces of gas bubbles, liquids, or solid materials wettable, while hydrophilic surfaces can be turned hydrophobic. These properties, among others, make hydrophobins of interest for medical and technical applications. For instance, hydrophobins can be used to disperse hydrophobic materials; to stabilize foam in food products; and to immobilize enzymes, peptides, antibodies, cells, and anorganic molecules on surfaces. At the same time, they may be used to prevent binding of molecules. Furthermore, hydrophobins have therapeutic value as immunomodulators and can been used to produce recombinant proteins.

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“…z j is the height (not in the coordinates of the unit cell). The folded structure of HFBIII, and thus the positions of the individual atoms, is not known, but because monomers of both HFBI (Hakanpä ä et al, 2006) and HFBII (Hakanpä ä , Paananen, Askolin et al, 2004) are rather spherical, HFBIII was approximated by a sphere. The HFBIII spheres were generated in various hexagonal space groups and the number, position and radius of the spheres were varied.…”

Section: Modellingmentioning

confidence: 99%

“…A similar phenomenom is also observed with three-dimensional single crystals. According to protein-crystallography studies, HFBI Hakanpä ä et al, 2006) and HFBII (Hakanpä ä , Paananen, Askolin et al, 2004;Hakanpä ä , Parkkinen, Hakulinen et al, 2004) can crystallize into different crystal structures depending on the conditions, i.e. with salts or detergents.…”

Section: Figurementioning

confidence: 99%

Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

Kisko¹,

Szilvay²,

Vuorimaa³

et al. 2007

J Appl Crystallogr

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Hydrophobins are a group of small amphiphilic proteins which are known to self-assemble on interfaces. They contain eight conserved cysteine residues, which make four disulfide bridges. A new hydrophobin protein, HFBIII, from the fungus Trichoderma reesei contains one extra cysteine residue, giving the protein a naturally reactive site. The self-assembly of hydrophobin protein HFBIII was studied using grazing-incidence X-ray diffraction and reflectivity. HFBIII self-assembles into a hexagonally ordered monolayer at an air/water interface and also forms crystalline coatings on a silicon substrate. The lattice constants for the hexagonal coatings are a = b = 56.5 Å , = 120 . The selfassembled structure in the HFBIII film is very similar to those formed by two other T. reesei hydrophobins, HFBI and HFBII.

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Two crystal structures of Trichoderma reesei hydrophobin HFBI—The structure of a protein amphiphile with and without detergent interaction

Cited by 154 publications

References 47 publications

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Applications of hydrophobins: current state and perspectives

Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

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