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

Automated summary

Zwitterionic peptides with neutral amino acid spacers of varying hydrophobicities were studied for their antifouling properties. Results showed that the hydrophilicity of the spacers affected the structure and performance of the peptide-modified surface. Serine spacers improved antifouling performance, while leucine spacers increased protein adhesion and reduced performance.