Selective and Controllable Trapping of Single Proteins in Nanopores Using Reversible Covalent Bonds.

ABSTRACT: Analysis of individual proteins using nanopores makes it possible to determine their size and shape in a label-free approach, within minutes, and from μL sample volumes. Short residence times of proteins in the nanopore, high electrical current noise, and bandwidth limitations of the recording electronics during resistive pulse recordings, however, limit the accuracy of size and shape analysis of individual proteins. The work presented here introduces a polymer surface coating of solid-state nanopores to minimize nonspecific interactions of proteins with the nanopore wall while functionalizing it covalently with phenylboronic acid (PBA) groups. These PBA groups make it possible to trap selectively glycated proteins by taking advantage of the formation of reversible covalent bonds between P

SUBMITTER: Li Y 

PROVIDER: S-EPMC12810480 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature