Lubricin-Inspired Loop Zwitterionic Peptide for Fabrication of Superior Antifouling Surfaces

Biofouling represents great challenges in many applications, and zwitterionic peptides have been a promising candidate due to their biocompatibility and excellent antifouling performance. Inspired by lubricin, we designed a loop-like zwitterionic peptide and investigated the effect of conformation (linear or loop) on the antifouling properties using a combination of surface plasma resonance (SPR), surface force apparatus (SFA), and all atomistic molecular dynamics (MD) simulation techniques. Our results demonstrate that the loop-like zwitterionic peptides perform better in resisting the adsorption of proteins and bacteria. SFA measurements show that the loop-like peptides reduce the adhesion between the modified surface and the modeling foulant lysozyme. All atomistic MD simulations reveal that the loop-like zwitterionic peptides are more rigid than the linear-like zwitterionic peptides and avoid the penetration of the terminus into the foulants, which lower the interaction between the zwitterionic peptides and foulants. Besides, the loop-like zwitterionic peptides avoid the aggregation of the chains and bind more water, improving the hydrophilicity and antifouling performance. Altogether, this study provides a more comprehensive understanding of the conformation effect of zwitterionic peptides on their antifouling properties, which may contribute to designing novel antifouling materials in various biomedical applications.

Automated summary

Zwitterionic peptides with loop-like structures exhibit better antifouling properties by resisting protein and bacteria adsorption, being more rigid compared to linear-like peptides, reducing interaction with foulants, improving hydrophilicity, and avoiding chain aggregation. This study provides a comprehensive understanding of the conformation effect of zwitterionic peptides, which may contribute to the design of novel antifouling materials in various biomedical applications.