ArticleProtein science : a publication of the Protein Society2010
Interaction of an ionic complementary peptide with a hydrophobic graphite surface.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Residue-Specific Dock-Loosen-Unfold Mechanism of GB1 on Nanoparticle Surfaces Revealed by Kinetic and Φ-Value Analysis.Biomolecules · 2026Article
- Recent Advances of Studies on Cell-Penetrating Peptides Based on Molecular Dynamics Simulations.Cells · 2022Review
- Mechanisms of the self-assembly of EAK16-family peptides into fibrillar and globular structures: molecular dynamics simulations from nano- to micro-seconds.European biophysics journal : EBJ · 2015Article
- All-atom molecular dynamics study of EAK16 peptide: the effect of pH on single-chain conformation, dimerization and self-assembly behavior.European biophysics journal : EBJ · 2014Article
- Efficient and Unbiased Sampling of Biomolecular Systems in the Canonical Ensemble: A Review of Self-Guided Langevin Dynamics.Advances in chemical physics · 2012Article
- Force-momentum-based self-guided Langevin dynamics: a rapid sampling method that approaches the canonical ensemble.The Journal of chemical physics · 2011Article
- Diffusion of hydrophobin proteins in solution and interactions with a graphite surface.BMC biophysics · 2011Article
- Interaction of an ionic complementary peptide with a hydrophobic graphite surface.Protein science : a publication of the Protein Society · 2010Article
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3 authors.
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Abstract
Protein adsorption on a surface plays an important role in biomaterial science and medicine. It is strongly related to the interaction between the protein residues and the surface. Here we report all-atom molecular dynamics simulations of the adsorption of an ionic complementary peptide, EAK16-II, to the hydrophobic highly ordered pyrolytic graphite surface. We find that, the hydrophobic interaction is the main force to govern the adsorption, and the peptide interchain electrostatic interaction affects the adsorption rate. Under neutral pH condition, the interchain electrostatic attraction facilitates the adsorption, whereas under acidic and basic conditions, because of the protonation and deprotonation of glutamic acid and lysine residues, respectively, the resulting electrostatic repulsion slows down the adsorption. We also found that under basic condition, during the adsorption peptide Chain II will be up against a choice to adsorb to the surface through the hydrophobic interaction or to form a temporary hydrophobic core with the deposited peptide Chain I. These results provide a basis for understanding some of the fundamental interactions governing peptide adsorption on the surface, which can shed new light on novel applications, such as the design of implant devices and drug delivery materials.
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