Large and Stable Nanopores Formed by Complement Component 9 for Characterizing Single Folded Proteins.

ABSTRACT: Biological nanopores offer a promising approach for single-molecule analysis of nucleic acids, peptides, and proteins. The work presented here introduces a biological nanopore formed by the self-assembly of complement component 9 (C9). This exceptionally large and cylindrical protein pore is composed of 20 ± 4 monomers of C9 resulting in a diameter of 10 ± 4 nm and an effective pore length of 13 nm. These poly(C9) pores remain stable for up to 30 min without indications of gating, flickering, or clogging across a range of transmembrane voltages (-150 to +150 mV) and ionic strengths (50 to 1000 mM). At physiologic pH, the ring-shaped distribution of negative and positive surface charges in the lumen of the pore enables capture of analyte proteins by electro-osmotic flow and leads to residen

SUBMITTER: Chanakul W 

PROVIDER: S-EPMC11823641 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature