Peptide adsorption on the hydrophobic surface: A free energy perspective

详细信息    查看全文

• 作者：Yuebiao Sheng^a ; ^b ; ^{syb@nju.edu.cn"" rel=""nofollow} ; Wei Wang^a ; P. Chen^b ; ^{p4chen@uwaterloo.ca"" rel=""nofollow}
• 关键词：Molecular dynamics ; Protein adsorption ; Ionic complementary peptide ; Adsorption free energy
• 刊名：Journal of Molecular Structure
• 出版年：2011
• 出版时间：31 May 2011
• 年：2011
• 卷：995
• 期：1-3
• 页码：142-147
• 全文大小：1221 K

文摘

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.