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Type: Journal article
Title: Molecular-level understanding of the adsorption mechanism of a graphite-binding peptide at the water/graphite interface
Author: Penna, M.
Mijajlovic, M.
Tamerler, C.
Biggs, M.
Citation: Soft matter, 2015; 11(26):5192-5203
Publisher: Royal Society of Chemistry
Issue Date: 2015
ISSN: 1744-683X
Statement of
M. J. Penna, M. Mijajlovic, C. Tamerler and M. J. Biggs
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.
Keywords: Graphite; Water; Peptides; Diffusion; Protein Conformation; Adsorption; Hydrogen Bonding; Surface Properties; Thermodynamics; Molecular Dynamics Simulation; Hydrophobic and Hydrophilic Interactions
Rights: © The Royal Society of Chemistry 2015
RMID: 0030028209
DOI: 10.1039/c5sm00123d
Grant ID:
Appears in Collections:Chemical Engineering publications

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