Affiliation:
1. State Key Laboratory of Chemo/Bio‐Sensing and Chemometrics School of Biomedical Sciences Hunan University Changsha Hunan 410082 P. R. China
2. College of Biology Hunan University Changsha Hunan 410082 P. R. China
3. Shenzhen International Institute for Biomedical Research Longhua District Shenzhen Guangdong 518116 P. R. China
Abstract
AbstractAs an important noncovalent interaction, cation–π interaction plays an essential role in a broad area of biology and chemistry. Despite extensive studies in protein stability and molecular recognition, the utilization of cation–π interaction as a major driving force to construct supramolecular hydrogel remains uncharted. Here, a series of peptide amphiphiles are designed with cation–π interaction pairs that can self‐assemble into supramolecular hydrogel under physiological condition. The influence of cation–π interaction is thoroughly investigated on peptide folding propensity, morphology, and rigidity of the resultant hydrogel. Computational and experimental results confirm that cation–π interaction could serve as a major driving force to trigger peptide folding, resultant β‐hairpin peptide self‐assembled into fibril‐rich hydrogel. Furthermore, the designed peptides exhibit high efficacy on cytosolic protein delivery. As the first case of using cation–π interactions to trigger peptide self‐assembly and hydrogelation, this work provides a novel strategy to generate supramolecular biomaterials.
Subject
Biomaterials,Biotechnology,General Materials Science,General Chemistry
Cited by
10 articles.
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