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Ley K, Christofferson A, Penna M, et al. Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Front Mol Biosci. 2015;2:64doi: 10.3389/fmolb.2015.00064.
Ley, K., Christofferson, A., Penna, M., Winkler, D., Maclaughlin, S., & Yarovsky, I. (2015). Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Frontiers in molecular biosciences, 264. https://doi.org/10.3389/fmolb.2015.00064
Ley, Kamron, et al. "Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin." Frontiers in molecular biosciences vol. 2 (2015): 64. doi: https://doi.org/10.3389/fmolb.2015.00064
Ley K, Christofferson A, Penna M, Winkler D, Maclaughlin S, Yarovsky I. Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Front Mol Biosci. 2015 Nov 16;2:64. doi: 10.3389/fmolb.2015.00064. eCollection 2015. PMID: 26636091; PMCID: PMC4644811.
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Front Mol Biosci. 2015 Nov 16;2:64. doi: 10.3389/fmolb.2015.00064. eCollection 2015.

Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin.

Frontiers in molecular biosciences

Kamron Ley, Andrew Christofferson, Matthew Penna, Dave Winkler, Shane Maclaughlin, Irene Yarovsky

Affiliations

  1. Health Innovations Research Institute and School of Aerospace, Mechanical and Manufacturing Engineering, RMIT University Melbourne, VIC, Australia.
  2. Health Innovations Research Institute and School of Aerospace, Mechanical and Manufacturing Engineering, RMIT University Melbourne, VIC, Australia ; Australian Research Council (ARC) Research Hub for Australian Steel Manufacturing Wollongong, NSW, Australia.
  3. CSIRO, Manufacturing Flagship Clayton, VIC, Australia ; Institute of Pharmaceutical Science, Monash University Parkville, VIC, Australia ; Institute for Molecular Science, Latrobe University Bundoora, VIC, Australia.
  4. Australian Research Council (ARC) Research Hub for Australian Steel Manufacturing Wollongong, NSW, Australia ; BlueScope Steel Research Laboratories Port Kembla, NSW, Australia.

PMID: 26636091 PMCID: PMC4644811 DOI: 10.3389/fmolb.2015.00064

Abstract

The class I hydrophobin EAS is part of a family of small, amphiphilic fungal proteins best known for their ability to self-assemble into stable monolayers that modify the hydrophobicity of a surface to facilitate further microbial growth. These proteins have attracted increasing attention for industrial and biomedical applications, with the aim of designing surfaces that have the potential to maintain their clean state by resisting non-specific protein binding. To gain a better understanding of this process, we have employed all-atom molecular dynamics to study initial stages of the spontaneous adsorption of monomeric EAS hydrophobin on fully hydroxylated silica, a commonly used industrial and biomedical substrate. Particular interest has been paid to the Cys3-Cys4 loop, which has been shown to exhibit disruptive behavior in solution, and the Cys7-Cys8 loop, which is believed to be involved in the aggregation of EAS hydrophobin at interfaces. Specific and water mediated interactions with the surface were also analyzed. We have identified two possible binding motifs, one which allows unfolding of the Cys7-Cys8 loop due to the surfactant-like behavior of the Cys3-Cys4 loop, and another which has limited unfolding due to the Cys3-Cys4 loop remaining disordered in solution. We have also identified intermittent interactions with water which mediate the protein adsorption to the surface, as well as longer lasting interactions which control the diffusion of water around the adsorption site. These results have shown that EAS behaves in a similar way at the air-water and surface-water interfaces, and have also highlighted the need for hydrophilic ligand functionalization of the silica surface in order to prevent the adsorption of EAS hydrophobin.

Keywords: anti-fouling; biofouling; hydrophobin; molecular dynamics; protein adsorption; silica surface

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