Self-assembled bilayers from the protein HFBII hydrophobin: Nature of the adhesion energy

Research output: Contribution to journalArticlepeer-review

Standard

Self-assembled bilayers from the protein HFBII hydrophobin : Nature of the adhesion energy. / Basheva, Elka S.; Kralchevsky, Peter A.; Danov, Krassimir D.; Stoyanov, Simeon D.; Blijdenstein, Theo B J; Pelan, Eddie G.; Lips, Alex.

In: Langmuir, Vol. 27, No. 8, 19.04.2011, p. 4481-4488.

Research output: Contribution to journalArticlepeer-review

Harvard

Basheva, ES, Kralchevsky, PA, Danov, KD, Stoyanov, SD, Blijdenstein, TBJ, Pelan, EG & Lips, A 2011, 'Self-assembled bilayers from the protein HFBII hydrophobin: Nature of the adhesion energy', Langmuir, vol. 27, no. 8, pp. 4481-4488. https://doi.org/10.1021/la2001943

APA

Basheva, E. S., Kralchevsky, P. A., Danov, K. D., Stoyanov, S. D., Blijdenstein, T. B. J., Pelan, E. G., & Lips, A. (2011). Self-assembled bilayers from the protein HFBII hydrophobin: Nature of the adhesion energy. Langmuir, 27(8), 4481-4488. https://doi.org/10.1021/la2001943

Vancouver

Basheva ES, Kralchevsky PA, Danov KD, Stoyanov SD, Blijdenstein TBJ, Pelan EG et al. Self-assembled bilayers from the protein HFBII hydrophobin: Nature of the adhesion energy. Langmuir. 2011 Apr 19;27(8):4481-4488. https://doi.org/10.1021/la2001943

Author

Basheva, Elka S. ; Kralchevsky, Peter A. ; Danov, Krassimir D. ; Stoyanov, Simeon D. ; Blijdenstein, Theo B J ; Pelan, Eddie G. ; Lips, Alex. / Self-assembled bilayers from the protein HFBII hydrophobin : Nature of the adhesion energy. In: Langmuir. 2011 ; Vol. 27, No. 8. pp. 4481-4488.

Bibtex

@article{8620484a86174a7baa5b138f0dd73491,
title = "Self-assembled bilayers from the protein HFBII hydrophobin: Nature of the adhesion energy",
abstract = "The hydrophobins are a class of amphiphilic proteins which spontaneously adsorb at the air/water interface and form elastic membranes of high mechanical strength as compared to other proteins. The mechanism of hydrophobin adhesion is of interest for fungal biology and for various applications in electronics, medicine, and food industry. We established that the drainage of free foam films formed from HFBII hydrophobin solutions ends with the appearance of a 6 nm thick film, which consists of two layers of protein molecules, that is, it is a self-assembled bilayer (S-bilayer), with hydrophilic domains pointing inward and hydrophobic domains pointing outward. Its formation is accompanied by a considerable energy gain, which is much greater than that typically observed with free liquid films. The experiments at different pH show that this attraction between the {"}hydrophilic{"} parts of the HFBII molecules is dominated by the short-range hydrophobic interaction rather than by the patch-charge electrostatic attraction.",
author = "Basheva, {Elka S.} and Kralchevsky, {Peter A.} and Danov, {Krassimir D.} and Stoyanov, {Simeon D.} and Blijdenstein, {Theo B J} and Pelan, {Eddie G.} and Alex Lips",
year = "2011",
month = apr,
day = "19",
doi = "10.1021/la2001943",
language = "English",
volume = "27",
pages = "4481--4488",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "8",

}

RIS

TY - JOUR

T1 - Self-assembled bilayers from the protein HFBII hydrophobin

T2 - Nature of the adhesion energy

AU - Basheva, Elka S.

AU - Kralchevsky, Peter A.

AU - Danov, Krassimir D.

AU - Stoyanov, Simeon D.

AU - Blijdenstein, Theo B J

AU - Pelan, Eddie G.

AU - Lips, Alex

PY - 2011/4/19

Y1 - 2011/4/19

N2 - The hydrophobins are a class of amphiphilic proteins which spontaneously adsorb at the air/water interface and form elastic membranes of high mechanical strength as compared to other proteins. The mechanism of hydrophobin adhesion is of interest for fungal biology and for various applications in electronics, medicine, and food industry. We established that the drainage of free foam films formed from HFBII hydrophobin solutions ends with the appearance of a 6 nm thick film, which consists of two layers of protein molecules, that is, it is a self-assembled bilayer (S-bilayer), with hydrophilic domains pointing inward and hydrophobic domains pointing outward. Its formation is accompanied by a considerable energy gain, which is much greater than that typically observed with free liquid films. The experiments at different pH show that this attraction between the "hydrophilic" parts of the HFBII molecules is dominated by the short-range hydrophobic interaction rather than by the patch-charge electrostatic attraction.

AB - The hydrophobins are a class of amphiphilic proteins which spontaneously adsorb at the air/water interface and form elastic membranes of high mechanical strength as compared to other proteins. The mechanism of hydrophobin adhesion is of interest for fungal biology and for various applications in electronics, medicine, and food industry. We established that the drainage of free foam films formed from HFBII hydrophobin solutions ends with the appearance of a 6 nm thick film, which consists of two layers of protein molecules, that is, it is a self-assembled bilayer (S-bilayer), with hydrophilic domains pointing inward and hydrophobic domains pointing outward. Its formation is accompanied by a considerable energy gain, which is much greater than that typically observed with free liquid films. The experiments at different pH show that this attraction between the "hydrophilic" parts of the HFBII molecules is dominated by the short-range hydrophobic interaction rather than by the patch-charge electrostatic attraction.

UR - http://www.scopus.com/inward/record.url?scp=79953863253&partnerID=8YFLogxK

U2 - 10.1021/la2001943

DO - 10.1021/la2001943

M3 - Article

C2 - 21413726

AN - SCOPUS:79953863253

VL - 27

SP - 4481

EP - 4488

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 8

ER -