Mussel-Inspired Cation-π Interactions: Wet Adhesion and Biomimetic Materials

Cation-pi interaction is one of the most important noncovalent interactions identified in biosystems, which has been proven to play an essential role in the strong adhesion of marine mussels. In addition to the well-known catecholic amino acid, l-3,4-dihydroxyphenylalanine, mussel foot proteins are rich in various aromatic moieties (e.g., tyrosine, phenylalanine, and tryptophan) and cationic residues (e.g., lysine, arginine, and histidine), which favor a series of short-range cation-pi interactions with adjustable strengths, serving as a prototype for the development of high-performance underwater adhesives. This work highlights our recent advances in understanding and utilizing cation-pi interactions in underwater adhesives, focusing on three aspects: (1) the investigation of the cation-pi interaction mechanisms in mussel foot proteins via force-measuring techniques; (2) the modulation of cation-pi interactions in mussel mimetic polymers with the variation of cations, anions, and aromatic groups; (3) the design of wet adhesives based on these revealed principles, leading to functional materials in the form of films, coacervates, and hydrogels with biomedical and engineering applications. This review provides valuable insights into the development and optimization of smart materials based on cation-pi interactions.

Automated summary

This article discusses the importance of cation-pi interactions in underwater adhesives, with a focus on their use in mussel foot proteins and mimetic polymers. By understanding the mechanisms and modulation of cation-pi interactions, functional materials with biomedical and engineering applications can be developed.