Structural Hierarchy in Molecular Films of Two Class II Hydrophobins

Paananen, Arja; Vuorimaa, Elina; Torkkeli, Mika; Penttilä, Merja; Kauranen, Martti; Ikkala, Olli; Lemmetyinen, Helge; Serimaa, Ritva; Linder, Markus B.

doi:10.1021/bi034031t

Cited by 120 publications

(148 citation statements)

References 27 publications

Supporting

Mentioning

137

Contrasting

Order By: Relevance

“…7a) ). The mean molecular area of HFBI was, as has been reported earlier,~250 Å 2 (~2.5 nm 2 ) (Paananen et al, 2003). The isotherm of HGFI was not as steep as that of HFBI.…”

Section: Afm Of Rodlet Layer and Langmuir Filmssupporting

confidence: 79%

“…The formation of class I hydrophobin layers has been found to lead to a rodlet-like mosaic pattern that resembles amyloid fibrils, whereas the aggregates of class II hydrophobins are non-amyloidal and needle-like (Hakanpää et al, 2006). Langmuir-Blodgett (LB) films of class II hydrophobins HFBI and HFBII have been studied, and atomic force microscopy (AFM) images of them show highly ordered 2D crystalline structures (Paananen et al, 2003;Szilvay et al, 2007). There are, to our knowledge, no previous reports on Langmuir film structures for class I hydrophobins.…”

Section: Introductionmentioning

confidence: 99%

“…Analytical-grade chemicals and MilliQ water were used. HFBI pressure-area isotherms were made as controls as described elsewhere (Paananen et al, 2003). Lyophilized HGFI was dissolved in water to a concentration of 27 mM, and 40 ml of the solution was spread on the subphase.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Protein HGFI from the edible mushroom Grifola frondosa is a novel 8 kDa class I hydrophobin that forms rodlets in compressed monolayers

Zhang

Szilvay

et al. 2008

Microbiology

Self Cite

View full text Add to dashboard Cite

Hydrophobins are a group of low-molecular-mass, cysteine-rich proteins that have unusual biophysical properties. They are highly surface-active and can self-assemble at hydrophobic-hydrophilic interfaces, forming surface layers that are able to reverse the hydropathy of surfaces. Here we describe a novel hydrophobin from the edible mushroom Grifola frondosa, which was named HGFI and belongs to class I. The hydrophobin gene was identified during sequencing of random clones from a cDNA library, and the corresponding protein was isolated as a hot SDS-insoluble aggregate from the cell wall. The purified HGFI was found to have 83 amino acids. The protein sequence deduced from the cDNA sequence had 107 amino acids, from which a 24 aa signal sequence had been cleaved off in the mature protein. This signal sequence was 5 aa longer than had been predicted on the basis of signal peptide analysis of the cDNA. Rodlet mosaic structures were imaged using atomic force microscopy (AFM) on mica surfaces after drying-down HGFI solutions. Using Langmuir films we were also able to take images of both the hydrophobic and hydrophilic sides of films formed at the air-water interface. No distinct structure was observed in films compressed once, but in films compressed several times rodlet structures could be seen. Most rodlets were aligned in the same direction, indicating that formation of rodlets may be promoted during compression of the monolayer.

show abstract

“…7a) ). The mean molecular area of HFBI was, as has been reported earlier,~250 Å 2 (~2.5 nm 2 ) (Paananen et al, 2003). The isotherm of HGFI was not as steep as that of HFBI.…”

Section: Afm Of Rodlet Layer and Langmuir Filmssupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Protein HGFI from the edible mushroom Grifola frondosa is a novel 8 kDa class I hydrophobin that forms rodlets in compressed monolayers

Zhang

Szilvay

et al. 2008

Microbiology

Self Cite

View full text Add to dashboard Cite

show abstract

“…[44][45][46] Fluorolink F10 (F10/A-ammonium salt, F10 in the text) was obtained from Solvay Specialty Polymers (Italy). The reagents (octadecylmercaptan, dodecane, ethylene glycol, diiodomethane) and solvents ( n -hexane, 2-propanol, and methanol) were purchased from Sigma-Aldrich and used without further purifi cation.…”

Section: Methodsmentioning

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…Hydrophobins also form foams very easily [10,11] and adsorb to various surfaces [4,[12][13][14][15]. At the air-water interface hydrophobins self-assemble into nanoscale structures, such as hexagonally ordered crystalline monolayers [9,16,17] or randomly aligned rodlets [18,19].…”

Section: Introductionmentioning

confidence: 99%

The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reesei

Szilvay¹,

Kisko²,

Serimaa³

2007

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Hydrophobins are small fungal surface active proteins that self-assemble at interfaces into films with nanoscale structures. The hydrophobin HFBI from Trichoderma reesei has been shown to associate in solution into tetramers but the role of this association on the function of HFBI has remained unclear. We produced two HFBI variants that showed a significant shift in solution association equilibrium towards the tetramer state. However, this enhanced solution association did not alter the surface properties of the variant HFBIs. The results show that there is not a strong relationship between HFBI solution association state and surface properties such as surface activity.

show abstract

Structural Hierarchy in Molecular Films of Two Class II Hydrophobins

Cited by 120 publications

References 27 publications

Protein HGFI from the edible mushroom Grifola frondosa is a novel 8 kDa class I hydrophobin that forms rodlets in compressed monolayers

Protein HGFI from the edible mushroom Grifola frondosa is a novel 8 kDa class I hydrophobin that forms rodlets in compressed monolayers

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

The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reesei

Contact Info

Product

Resources

About