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https://hdl.handle.net/2440/93013
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dc.contributor.author | Penna, M. | - |
dc.contributor.author | Mijajlovic, M. | - |
dc.contributor.author | Tamerler, C. | - |
dc.contributor.author | Biggs, M. | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | Soft Matter, 2015; 11(26):5192-5203 | - |
dc.identifier.issn | 1744-683X | - |
dc.identifier.issn | 1744-6848 | - |
dc.identifier.uri | http://hdl.handle.net/2440/93013 | - |
dc.description.abstract | The association of proteins and peptides with inorganic material has vast technological potential. An understanding of the adsorption of peptides at liquid/ solid interfaces on a molecular-level is fundamental to fully realising this potential. Combining our prior work along with the statistical analysis of 100+ molecular dynamics simulations of adsorption of an experimentally identified graphite binding peptide, GrBP5, at the water/graphite interface has been used here to propose a model for the adsorption of a peptide at a liquid/solid interface. This bottom-up model splits the adsorption process into three reversible phases: biased diffusion, anchoring and lockdown. Statistical analysis highlighted the distinct roles played by regions of the peptide studied here throughout the adsorption process: the hydrophobic domain plays a significant role in the biased diffusion and anchoring phases suggesting that the initial impetus for association between the peptide and the interface may be hydrophobic in origin; aromatic residues dominate the interaction between the peptide and the surface in the adsorbed state and the polar region in the middle of the peptide affords a high conformational flexibility allowing strongly interacting residues to maximise favourable interactions with the surface. Reversible adsorption was observed here, unlike in our prior work focused on a more strongly interacting surface. However, this reversibility is unlikely to be seen once the peptide– surface interaction exceeds 10 kcal mol-1. | - |
dc.description.statementofresponsibility | M. J. Penna, M. Mijajlovic, C. Tamerler and M. J. Biggs | - |
dc.language.iso | en | - |
dc.publisher | Royal Society of Chemistry | - |
dc.rights | © The Royal Society of Chemistry 2015 | - |
dc.source.uri | http://dx.doi.org/10.1039/c5sm00123d | - |
dc.subject | Graphite | - |
dc.subject | Water | - |
dc.subject | Peptides | - |
dc.subject | Diffusion | - |
dc.subject | Protein Conformation | - |
dc.subject | Adsorption | - |
dc.subject | Hydrogen Bonding | - |
dc.subject | Surface Properties | - |
dc.subject | Thermodynamics | - |
dc.subject | Molecular Dynamics Simulation | - |
dc.subject | Hydrophobic and Hydrophilic Interactions | - |
dc.title | Molecular-level understanding of the adsorption mechanism of a graphite-binding peptide at the water/graphite interface | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1039/c5sm00123d | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP130101714 | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 2 Chemical Engineering publications |
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