Discrimination and Translocation of Charged Proteinogenic Amino Acids through a Single-Walled Carbon Nanotube.

Nanopore sensing relies on associating the measured current signals with specific features of the target molecules. The diversity of amino acids presents significant challenges in detecting and sequencing peptides and proteins. The hollow and uniform tubular structure of single-walled carbon nanotubes (SWCNTs) makes them ideal candidates for nanopore sensors. Here, we demonstrate by molecular dynamics simulations the discrimination and translocation of charged proteinogenic amino acids through the nanopore sensor formed by inserting a SWCNT into lipid bilayers. Moreover, our analysis suggests that the current blockade is influenced not only by excluded atomic volume but also by noncovalent interactions between amino acids and SWCNT during similar helical translocation. The presence of noncovalent interactions enhances the understanding of current differences in nanopore translocation of molecules with similar excluded atomic volume. This finding provides new perspectives and applications for the optimal design of SWCNT nanopore sensors.