Effect of Hydrophobicity and Charge Separation on the Antifouling Properties of Surface-Tethered Zwitterionic Peptides

Zwitterionic peptides emerge as a class of highly effective antifouling material in wide range applications such biosensors, biomedical devices, and implants. We incorporated neutral amino acid spacers with different hydrophobicities, including serine (Ser), glycine (Gly), leucine (Leu), into zwitterionic lysine–glutamic repeating units investigated the structure performance peptide brushes by surface plasma resonance, force apparatus (SFA), all-atomistic molecular dynamics (MD) simulation techniques. Our results demonstrate that hydrophilicity alters peptide-modified surface. Hydrophilic Ser-inserted reduced interaction between monolayer protein foulants, while hydrophobic Leu significantly increased adhesion. SFA measurements show presence more would increase adhesion modeling foulant lysozyme, especially for spacers. MD simulations reveal hydrophilic Ser retain improve performance, Gly give rise to interchain cross-links. result monolayer, which leads dehydration reduces performances.