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

Publication year: 2021
Authors: Chuanxi Li 1,2, Yinqiang Xia 3, Chunjiang Liu 1, Renliang Huang 4, Wei Qi 1, Zhimin He 1, Rongxin Su 1,4

1 - State Key Laboratory of Chemical Engineering, Tianjin Key Laboratory of Membrane Science and Desalination Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, P. R. China
2 - Petrochemical Research Institute, PetroChina, Beijing 102206, P. R. China
3 - College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi 712100, P. R. China
4 - School of Marine Science and Technology, Tianjin University, Tianjin 300072, P. R. China

Published in: ACS Applied Materials & Interfaces, 2021, Vol. 13(35), p. 41978–41986
doi: 10.1021/acsami.1c09254

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.

MP-SPR keywords: antifouling, Au sensor slide, non-specific adsorption