Identification of Single Amino Acid Chiral and Positional Isomers Using an Electrostatically Asymmetric Nanopore.

ABSTRACT: Chirality is essential in nearly all biological organizations and chemical reactions but is rarely considered due to technical limitations in identifying L/D isomerization. Using OmpF, a membrane channel from Escherichia coli with an electrostatically asymmetric constriction zone, allows discriminating chiral amino acids in a single peptide. The heterogeneous distribution of charged residues in OmpF causes a strong lateral electrostatic field at the constriction. This laterally asymmetric constriction zone forces the sidechains of the peptides to specific orientations within OmpF, causing distinct ionic current fluctuations. Using statistical analysis of the respective ionic current variations allows distinguishing the presence and position of a single amino acid with different chir

SUBMITTER: Wang J 

PROVIDER: S-EPMC9413207 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature