An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport.

ABSTRACT: Reading the primary sequence directly using nanopores remains challenging due to the complex building blocks of 20 proteinogenic amino acids and the corresponding sophisticated structures. Compared to the uniformly negatively charged polynucleotides, biological nanopores hardly provide effective ionic current responses to all heterogeneously charged peptides under nearly physiological pH conditions. Herein, we precisely design a N226Q/S228K mutant aerolysin which creates a new electrostatic constriction named R3 in-between two natural sensing regions for controlling the capture and translocation of heterogeneously charged peptides. At nearly physiological pH, the decoration of positive charges at this constriction gives a large velocity of electroosmotic flow (EOF), leading to a maximum 8-

SUBMITTER: Niu H 

PROVIDER: S-EPMC8864703 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature