Molecular Simulation of Hydrophobin Adsorption at an Oil-Water Interface

Department of Chemistry and Centre for Scientific Computing, University of Warwick, Coventry CV4 7AL, UK.
Langmuir (Impact Factor: 4.46). 05/2012; 28(23):8730-6. DOI: 10.1021/la300777q
Source: PubMed


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 k(B)T (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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    • "Since protein surface activity and self-assembly at hydrophilic–hydrophobic interfaces is usually linked to denaturation of the individual molecules, in this work we study the stability of the hydrophobin HFBII in water, in a fluorinated solvent, and at the air/water interface, using Molecular Mechanics (MM) and Molecular Dynamics (MD) methods at a fully atomistic level, and adopting a simulation protocol formerly used by us [14] [15] [16] [17] [18] to model the conformational properties and stability of unlike proteins, in particular when adsorbed on solid biomaterial surfaces. The theoretical results will also be compared when possible with previous MD simulations, which used a coarse-grained model, yielding some chemical details for HFBI in water and at a water/octane interface [19], or a fully atomistic model in water and at a water/decane interface [20]. Furthermore, we report new circular dichroism (CD) data of HFBII in water and in an emulsion of a fluorinated solvent in order to compare these experimental data with the theoretical results. "
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    ABSTRACT: Hydrophobins are proteins of interest for numerous applications thanks to their unique conformational and surface properties and their ability to self-assemble at interfaces. Here we report fully atomistic molecular mechanics and molecular dynamics results together with circular dichroism experimental data, aimed to study the conformational properties of the hydrophobin HFBII in a fluorinated solvent in comparison with a water solution and/or at an aqueous/vacuum interface. Both the atomistic simulations and the circular dichroism data show the remarkable structural stability of HFBII at all scales in all these environments, with no significant structural change, although a small cavity is formed in the fluorinated solvent. The combination of theoretical calculations and circular dichroism data can describe in detail the protein conformation and flexibility in different solvents and/or at an interface, and constitutes a first step towards the study of their self-assembly.
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