Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei: Dissertation

Research output: ThesisDissertationCollection of Articles

1 Citation (Scopus)

Abstract

Hydrophobins are small surface active proteins that are produced by filamentous fungi. The surface activity of hydrophobin proteins leads to the formation of a film at the air-water interface and adsorption to surfaces. The formation of these hydrophobin films and coatings is important in many stages of fungal development. Furthermore, these properties make hydrophobins interesting for potential use in technical applications. The surfactant-like properties of hydrophobins from Trichoderma reesei were studied at the air-water interface, at solid surfaces, and in solution. The hydrophobin HFBI was observed to spontaneously form a cohesive film on a water drop. The film was imaged using atomic force microscopy from both sides, revealing a monomolecular film with a defined molecular structure. The use of hydrophobins as surface immobilization carriers for enzymes was studied using fusion proteins of HFBI or HFBII and an enzyme. Furthermore, site-specifically modified variants of HFBI were shown to retain their ability to self-assemble at interfaces and to be able to bind a second layer of proteins by biomolecular recognition. In order to understand the function of hydrophobins at interfaces, an understanding of their overall behavior and self-assembly is needed. HFBI and HFBII were shown to associate in solution into dimers and tetramers in a concentration-dependent manner. The association dynamics and protein-protein interactions of HFBI and HFBII were studied using Förster resonance energy transfer and size exclusion chromatography. It was shown that the surface activity of HFBI is not directly dependent on the formation of multimers in solution.
Original languageEnglish
QualificationDoctor Degree
Awarding Institution
  • University of Helsinki
Supervisors/Advisors
  • Linder, Markus, Supervisor, External person
Award date2 Nov 2007
Place of PublicationEspoo
Publisher
Print ISBNs978-951-38-7049-2
Electronic ISBNs978-951-38-7050-8
Publication statusPublished - 2007
MoE publication typeG5 Doctoral dissertation (article)

Fingerprint

Fungi
Self assembly
Proteins
Water
Size exclusion chromatography
Enzymes
Air
Surface-Active Agents
Dimers
Energy transfer
Molecular structure
1-(heptafluorobutyryl)imidazole
Monolayers
Atomic force microscopy
Fusion reactions
Association reactions
Adsorption
Coatings

Keywords

  • hydrophobin
  • protein self-assembly
  • protein adhesion
  • protein multimerization
  • surface active protein
  • Trichoderma reesei
  • HFBI
  • HFBII

Cite this

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title = "Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei: Dissertation",
abstract = "Hydrophobins are small surface active proteins that are produced by filamentous fungi. The surface activity of hydrophobin proteins leads to the formation of a film at the air-water interface and adsorption to surfaces. The formation of these hydrophobin films and coatings is important in many stages of fungal development. Furthermore, these properties make hydrophobins interesting for potential use in technical applications. The surfactant-like properties of hydrophobins from Trichoderma reesei were studied at the air-water interface, at solid surfaces, and in solution. The hydrophobin HFBI was observed to spontaneously form a cohesive film on a water drop. The film was imaged using atomic force microscopy from both sides, revealing a monomolecular film with a defined molecular structure. The use of hydrophobins as surface immobilization carriers for enzymes was studied using fusion proteins of HFBI or HFBII and an enzyme. Furthermore, site-specifically modified variants of HFBI were shown to retain their ability to self-assemble at interfaces and to be able to bind a second layer of proteins by biomolecular recognition. In order to understand the function of hydrophobins at interfaces, an understanding of their overall behavior and self-assembly is needed. HFBI and HFBII were shown to associate in solution into dimers and tetramers in a concentration-dependent manner. The association dynamics and protein-protein interactions of HFBI and HFBII were studied using F{\"o}rster resonance energy transfer and size exclusion chromatography. It was shown that the surface activity of HFBI is not directly dependent on the formation of multimers in solution.",
keywords = "hydrophobin, protein self-assembly, protein adhesion, protein multimerization, surface active protein, Trichoderma reesei, HFBI, HFBII",
author = "G{\'e}za Szilvay",
note = "Project code: 16352",
year = "2007",
language = "English",
isbn = "978-951-38-7049-2",
series = "VTT Publications",
publisher = "VTT Technical Research Centre of Finland",
number = "657",
address = "Finland",
school = "University of Helsinki",

}

Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei : Dissertation. / Szilvay, Géza.

Espoo : VTT Technical Research Centre of Finland, 2007. 69 p.

Research output: ThesisDissertationCollection of Articles

TY - THES

T1 - Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei

T2 - Dissertation

AU - Szilvay, Géza

N1 - Project code: 16352

PY - 2007

Y1 - 2007

N2 - Hydrophobins are small surface active proteins that are produced by filamentous fungi. The surface activity of hydrophobin proteins leads to the formation of a film at the air-water interface and adsorption to surfaces. The formation of these hydrophobin films and coatings is important in many stages of fungal development. Furthermore, these properties make hydrophobins interesting for potential use in technical applications. The surfactant-like properties of hydrophobins from Trichoderma reesei were studied at the air-water interface, at solid surfaces, and in solution. The hydrophobin HFBI was observed to spontaneously form a cohesive film on a water drop. The film was imaged using atomic force microscopy from both sides, revealing a monomolecular film with a defined molecular structure. The use of hydrophobins as surface immobilization carriers for enzymes was studied using fusion proteins of HFBI or HFBII and an enzyme. Furthermore, site-specifically modified variants of HFBI were shown to retain their ability to self-assemble at interfaces and to be able to bind a second layer of proteins by biomolecular recognition. In order to understand the function of hydrophobins at interfaces, an understanding of their overall behavior and self-assembly is needed. HFBI and HFBII were shown to associate in solution into dimers and tetramers in a concentration-dependent manner. The association dynamics and protein-protein interactions of HFBI and HFBII were studied using Förster resonance energy transfer and size exclusion chromatography. It was shown that the surface activity of HFBI is not directly dependent on the formation of multimers in solution.

AB - Hydrophobins are small surface active proteins that are produced by filamentous fungi. The surface activity of hydrophobin proteins leads to the formation of a film at the air-water interface and adsorption to surfaces. The formation of these hydrophobin films and coatings is important in many stages of fungal development. Furthermore, these properties make hydrophobins interesting for potential use in technical applications. The surfactant-like properties of hydrophobins from Trichoderma reesei were studied at the air-water interface, at solid surfaces, and in solution. The hydrophobin HFBI was observed to spontaneously form a cohesive film on a water drop. The film was imaged using atomic force microscopy from both sides, revealing a monomolecular film with a defined molecular structure. The use of hydrophobins as surface immobilization carriers for enzymes was studied using fusion proteins of HFBI or HFBII and an enzyme. Furthermore, site-specifically modified variants of HFBI were shown to retain their ability to self-assemble at interfaces and to be able to bind a second layer of proteins by biomolecular recognition. In order to understand the function of hydrophobins at interfaces, an understanding of their overall behavior and self-assembly is needed. HFBI and HFBII were shown to associate in solution into dimers and tetramers in a concentration-dependent manner. The association dynamics and protein-protein interactions of HFBI and HFBII were studied using Förster resonance energy transfer and size exclusion chromatography. It was shown that the surface activity of HFBI is not directly dependent on the formation of multimers in solution.

KW - hydrophobin

KW - protein self-assembly

KW - protein adhesion

KW - protein multimerization

KW - surface active protein

KW - Trichoderma reesei

KW - HFBI

KW - HFBII

M3 - Dissertation

SN - 978-951-38-7049-2

T3 - VTT Publications

PB - VTT Technical Research Centre of Finland

CY - Espoo

ER -

Szilvay G. Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei: Dissertation. Espoo: VTT Technical Research Centre of Finland, 2007. 69 p.