Adhesion Properties of Freestanding Hydrophobin Bilayers

Hendrik Hähl (Corresponding Author), Jose Nabor Vargas, Michael Jung, Alessandra Griffo, Päivi Laaksonen, Michael Lienemann, Karin Jacobs, Ralf Seemann, Jean Baptiste Fleury (Corresponding Author)

    Research output: Contribution to journalArticleResearchpeer-review

    Abstract

    Hydrophobins are a family of small-sized proteins featuring a distinct hydrophobic patch on the protein's surface, rendering them amphiphilic. This particularity allows hydrophobins to self-assemble into monolayers at any hydrophilic/hydrophobic interface. Moreover, stable pure protein bilayers can be created from two interfacial hydrophobin monolayers by contacting either their hydrophobic or their hydrophilic sides. In this study, this is achieved via a microfluidic approach, in which also the bilayers' adhesion energy can be determined. This enables us to study the origin of the adhesion of hydrophobic and hydrophilic core bilayers made from the class II hydrophobins HFBI and HFBII. Using different fluid media in this setup and introducing genetically modified variants of the HFBI molecule, the different force contributions to the adhesion of the bilayer sheets are studied. It was found that in the hydrophilic contact situation, the adhesive interaction was higher than that in the hydrophobic contact situation and could be even enhanced by reducing the contributions of electrostatic interactions. This effect indicates that the van der Waals interaction is the dominant contribution that explains the stability of the observed bilayers.

    LanguageEnglish
    Pages8542-8549
    Number of pages8
    JournalLangmuir
    Volume34
    Issue number29
    DOIs
    Publication statusPublished - 24 Jul 2018
    MoE publication typeNot Eligible

    Fingerprint

    adhesion
    Adhesion
    proteins
    Proteins
    Monolayers
    interactions
    Coulomb interactions
    Microfluidics
    adhesives
    Adhesives
    Membrane Proteins
    electrostatics
    Molecules
    Fluids
    fluids
    molecules
    1-(heptafluorobutyryl)imidazole
    energy

    OKM Publication Types

    • A1 Refereed journal article

    OKM Open Access Status

    • 0 Not Open Access

    ASJC Scopus subject areas

    • Materials Science(all)
    • Condensed Matter Physics
    • Surfaces and Interfaces
    • Spectroscopy
    • Electrochemistry

    Cite this

    Hähl, H., Vargas, J. N., Jung, M., Griffo, A., Laaksonen, P., Lienemann, M., ... Fleury, J. B. (2018). Adhesion Properties of Freestanding Hydrophobin Bilayers. Langmuir, 34(29), 8542-8549. https://doi.org/10.1021/acs.langmuir.8b00575
    Hähl, Hendrik ; Vargas, Jose Nabor ; Jung, Michael ; Griffo, Alessandra ; Laaksonen, Päivi ; Lienemann, Michael ; Jacobs, Karin ; Seemann, Ralf ; Fleury, Jean Baptiste. / Adhesion Properties of Freestanding Hydrophobin Bilayers. In: Langmuir. 2018 ; Vol. 34, No. 29. pp. 8542-8549.
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    abstract = "Hydrophobins are a family of small-sized proteins featuring a distinct hydrophobic patch on the protein's surface, rendering them amphiphilic. This particularity allows hydrophobins to self-assemble into monolayers at any hydrophilic/hydrophobic interface. Moreover, stable pure protein bilayers can be created from two interfacial hydrophobin monolayers by contacting either their hydrophobic or their hydrophilic sides. In this study, this is achieved via a microfluidic approach, in which also the bilayers' adhesion energy can be determined. This enables us to study the origin of the adhesion of hydrophobic and hydrophilic core bilayers made from the class II hydrophobins HFBI and HFBII. Using different fluid media in this setup and introducing genetically modified variants of the HFBI molecule, the different force contributions to the adhesion of the bilayer sheets are studied. It was found that in the hydrophilic contact situation, the adhesive interaction was higher than that in the hydrophobic contact situation and could be even enhanced by reducing the contributions of electrostatic interactions. This effect indicates that the van der Waals interaction is the dominant contribution that explains the stability of the observed bilayers.",
    author = "Hendrik H{\"a}hl and Vargas, {Jose Nabor} and Michael Jung and Alessandra Griffo and P{\"a}ivi Laaksonen and Michael Lienemann and Karin Jacobs and Ralf Seemann and Fleury, {Jean Baptiste}",
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    Hähl, H, Vargas, JN, Jung, M, Griffo, A, Laaksonen, P, Lienemann, M, Jacobs, K, Seemann, R & Fleury, JB 2018, 'Adhesion Properties of Freestanding Hydrophobin Bilayers' Langmuir, vol. 34, no. 29, pp. 8542-8549. https://doi.org/10.1021/acs.langmuir.8b00575

    Adhesion Properties of Freestanding Hydrophobin Bilayers. / Hähl, Hendrik (Corresponding Author); Vargas, Jose Nabor; Jung, Michael; Griffo, Alessandra; Laaksonen, Päivi; Lienemann, Michael; Jacobs, Karin; Seemann, Ralf; Fleury, Jean Baptiste (Corresponding Author).

    In: Langmuir, Vol. 34, No. 29, 24.07.2018, p. 8542-8549.

    Research output: Contribution to journalArticleResearchpeer-review

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    AU - Jacobs, Karin

    AU - Seemann, Ralf

    AU - Fleury, Jean Baptiste

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    Hähl H, Vargas JN, Jung M, Griffo A, Laaksonen P, Lienemann M et al. Adhesion Properties of Freestanding Hydrophobin Bilayers. Langmuir. 2018 Jul 24;34(29):8542-8549. https://doi.org/10.1021/acs.langmuir.8b00575