Molecular simulation of hydrophobin adsorption at an oil–water interface

David Cheung

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Hydrophobins are small, amphiphilic proteins expressed by strains of filamentous fungi. They fulfill a number of biological functions, often related to adsorption at hydrophobic interfaces, and have been investigated for a number of applications in materials science and biotechnology. In order to understand the biological function and applications of these proteins, a microscopic picture of the adsorption of these proteins at interfaces is needed. Using molecular dynamics simulations with a chemically detailed coarse-grained potential, the behavior of typical hydrophobins at the water–octane interface is studied. Calculation of the interfacial adsorption strengths indicates that the adsorption is essentially irreversible, with adsorption strengths of the order of 100 kBT (comparable to values determined for synthetic nanoparticles but significantly larger than small molecule surfactants and biomolecules). The protein structure at the interface is unchanged at the interface, which is consistent with the biological function of these proteins. Comparison of native proteins with pseudoproteins that consist of uniform particles shows that the surface structure of these proteins has a large effect on the interfacial adsorption strengths, as does the flexibility of the protein.
LanguageEnglish
Pages8730-8736
Number of pages7
JournalLangmuir
Volume28
Issue number23
DOIs
Publication statusPublished - 12 Jun 2012

Fingerprint

Oils
oils
proteins
Proteins
Adsorption
adsorption
Water
water
simulation
biotechnology
fungi
Biomolecules
octanes
Materials science
Biotechnology
materials science
Fungi
Surface-Active Agents
Surface structure
Interfaces (computer)

Keywords

  • hydrophobins
  • amphiphilic proteins
  • interfacial adsorption
  • water–octane interface

Cite this

Cheung, David. / Molecular simulation of hydrophobin adsorption at an oil–water interface. In: Langmuir. 2012 ; Vol. 28, No. 23. pp. 8730-8736.
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Molecular simulation of hydrophobin adsorption at an oil–water interface. / Cheung, David.

In: Langmuir, Vol. 28, No. 23, 12.06.2012, p. 8730-8736.

Research output: Contribution to journalArticle

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AB - Hydrophobins are small, amphiphilic proteins expressed by strains of filamentous fungi. They fulfill a number of biological functions, often related to adsorption at hydrophobic interfaces, and have been investigated for a number of applications in materials science and biotechnology. In order to understand the biological function and applications of these proteins, a microscopic picture of the adsorption of these proteins at interfaces is needed. Using molecular dynamics simulations with a chemically detailed coarse-grained potential, the behavior of typical hydrophobins at the water–octane interface is studied. Calculation of the interfacial adsorption strengths indicates that the adsorption is essentially irreversible, with adsorption strengths of the order of 100 kBT (comparable to values determined for synthetic nanoparticles but significantly larger than small molecule surfactants and biomolecules). The protein structure at the interface is unchanged at the interface, which is consistent with the biological function of these proteins. Comparison of native proteins with pseudoproteins that consist of uniform particles shows that the surface structure of these proteins has a large effect on the interfacial adsorption strengths, as does the flexibility of the protein.

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