Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore.

ABSTRACT: There are still unmet needs in finding new technologies for biomedical diagnostic and industrial applications. A technology allowing the analysis of size and sequence of short peptide molecules of only few molecular copies is still challenging. The fast, low-cost and label-free single-molecule nanopore technology could be an alternative for addressing these critical issues. Here, we demonstrate that the wild-type aerolysin nanopore enables the size-discrimination of several short uniformly charged homopeptides, mixed in solution, with a single amino acid resolution. Our system is very sensitive, allowing detecting and characterizing a few dozens of peptide impurities in a high purity commercial peptide sample, while conventional analysis techniques fail to do so.

SUBMITTER: Piguet F 

PROVIDER: S-EPMC5840376 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature