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• W2048111901 endingPage "147" @default.
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• W2048111901 abstract "Protein adsorption is a very attractive topic which relates to many novel applications in biomaterials, biotechnology and nanotechnology. Ionic complementary peptides are a group of novel nano-biomaterials with many biomedical applications. In this work, molecular dynamics simulations of the ionic-complementary peptide EAK16-II on a hydrophobic graphite surface were performed under neutral, acidic and basic solution conditions. Adsorption free energy contour maps were obtained by analyzing the dynamical trajectories. Hydrophobic interactions were found to govern the adsorption of the first peptide molecule, and both hydrophobic and electrostatic interactions contributed to the adsorption of the second peptide molecule. Especially under acidic and basic solution conditions, interplay existed among chain–chain hydrophobic, chain–surface hydrophobic and chain–chain electrostatic interactions during the adsorption of the second peptide molecule. Non-charged residues were found to lie on the graphite surface, while charged residue side-chains oriented towards the solution after the peptide deposited on the surface. These results provide a basis for understanding peptide adsorption on the hydrophobic surface under different solution conditions, which is useful for novel applications such as bioactive implant devices and drug delivery material design." @default.
• W2048111901 created "2016-06-24" @default.
• W2048111901 creator A5046597133 @default.
• W2048111901 creator A5063877684 @default.
• W2048111901 creator A5064672531 @default.
• W2048111901 date "2011-05-01" @default.
• W2048111901 modified "2023-09-23" @default.
• W2048111901 title "Peptide adsorption on the hydrophobic surface: A free energy perspective" @default.
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• W2048111901 doi "https://doi.org/10.1016/j.molstruc.2011.04.007" @default.
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