Chiral Selective Transport of Proteins by Cysteine-Enantiomer-Modified Nanopores

Chirality is an intriguing and intrinsic feature of life and is highly associated with many significant biological processes. However, whether it influences the translocation behavior of proteins remains unclear. Herein, based on biomimetic strategies, we made chiral nanopores modified with cysteine enantiomers, and studied the chirality gating effects on protein transport. The results show that protein is preferentially transported through nanopores modified with L-cysteine because of chiral interaction, indicating chirality strongly influences protein transport process. This study presents a new method for better understanding the role of chirality in selective protein transport processes and provides a convenient approach for studying protein chiral separation and targeted treatments.