Nanoscale interactions of arginine-containing dipeptide repeats with nuclear pore complexes as measured by transient scanning electrochemical microscopy.

ABSTRACT: The nuclear pore complex (NPC) plays imperative biological and biomedical roles as the sole gateway for molecular transport between the cytoplasm and nucleus of eukaryotic cells. The proteinous nanopore, however, can be blocked by arginine-containing polydipeptide repeats (DPRs) of proteins resulting from the disordered C9orf72 gene as a potential cause of serious neurological diseases. Herein, we report the new application of transient scanning electrochemical microscopy (SECM) to quantitatively characterize DPR-NPC interactions for the first time. Twenty repeats of neurotoxic glycine-arginine and proline-arginine in the NPC are quantified to match the number of phenylalanine-glycine (FG) units in hydrophobic transport barriers of the nanopore. The 1 : 1 stoichiometry supports the hypothe

SUBMITTER: Huang SH 

PROVIDER: S-EPMC11375788 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature