Molecular dynamics simulations of peptide adsorption on self-assembled monolayers

All-atom molecular dynamics simulations are performed to investigate the neuromedin-B peptide adsorption on the self-assembled monolayers (SAMs) of SH(CH2)10N+(CH3)2CH2CH(OH)CH2SO3- (SBT), SH(CH2)10OH and SH(CH2)10CH3. The force-distance profiles show that the surface resistance to peptide adsorption is mainly generated by the water molecules tightly bound to surfaces via hydrogen bonds (hydration water molecules); but surfaces themselves may also set an energy barrier for the approaching peptide. For the SBT-SAM, the surface first exerts a relatively high repulsive force and then a rather week attractive force on the approaching peptide; meanwhile the hydration water molecules exert a strong repulsive force on the peptide. Therefore, SBT-SAM has an excellent performance on resisting protein adsorption. For the OH-SAM and CH3-SAM, surfaces show low or little energy barrier but strong affinity to the peptide; and the hydration water molecules apply merely a repulsive force within a much narrower range and with lower intensity compared with the case for the SBT-SAM. The analysis of structural and dynamical properties of the peptide, surface and water indicates that possible factors contributing to surface resistance include the hydrogen-bond formation capability of surfaces, mobility of water molecules near surfaces, surface packing density and chain flexibility of SAMs. There are a large number of hydrogen bonds formed between the hydration water molecules and the functional groups of the SBT-SAM, which greatly lowers the mobility of water molecules near the surface. This tightly-bound water layer effectively reduces the direct contact between the surface and the peptide. Furthermore, the SBT-SAM also has a high flexibility and a low surface packing density, which allows water molecules to penetrate into the surface to form tightly-bound networks and therefore reduces the affinity between the peptide and the surface. The results show that the protein-resistant properties of the SAMs are in the decreasing order of SBT-SAM > OH-SAM > CH3-SAM, which provide mechanistic explanation on SBT materials' excellent anti-fouling performance.