Issue 18, 2022

Aerolysin nanopore-based identification of proteinogenic amino acids using a bipolar peptide probe

Abstract

Nanopore technology has attracted extensive attention due to its rapid, highly sensitive, and label-free performance. In this study, we aimed to identify proteinogenic amino acids using a wild-type aerolysin nanopore. Specifically, bipolar peptide probes were synthesised by linking four aspartic acid residues to the N-terminal and five arginine residues to the C-terminal of individual amino acids. With the help of the bipolar peptide carrier, 9 proteinogenic amino acids were reliably recognised based on current blockade and dwell time using an aerolysin nanopore. Furthermore, by changing the charge of the peptide probe, two of the five unrecognized amino acids above mentioned were identified. These findings promoted the application of aerolysin nanopores in proteinogenic amino acid recognition.

Graphical abstract: Aerolysin nanopore-based identification of proteinogenic amino acids using a bipolar peptide probe

Supplementary files

Article information

Article type
Paper
Submitted
29 Mar 2022
Accepted
05 Aug 2022
First published
11 Aug 2022
This article is Open Access
Creative Commons BY-NC license

Nanoscale Adv., 2022,4, 3883-3891

Aerolysin nanopore-based identification of proteinogenic amino acids using a bipolar peptide probe

Y. Ge, M. Cui, Q. Zhang, Y. Wang and D. Xi, Nanoscale Adv., 2022, 4, 3883 DOI: 10.1039/D2NA00190J

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