Spider venom peptides with unique fold selectively block Shaker-type potassium channels.

ABSTRACT: Natural toxins are highly effective at targeting ion channels with high selectivity and potency. To date, all identified spider venom peptide toxins that modulate voltage-gated potassium (K_V) channels inhibit Shab (K_V2) or Shal-related isoforms (K_V4) by interacting with their voltage-sensing domains. In this study, we report novel spider-derived pore-blocking toxins that selectively target Shaker-type (K_V1) channels with nanomolar potency. We isolated murinotoxins MnTx-1 and MnTx-2 from the orange baboon tarantula Pterinochilus murinus and sequenced them using a combination of Edman degradation, mass spectrometry, and venom gland nanopore transcriptomics. MnTx-1 was produced recombinantly, and its NMR solution structure was determined. Although M

SUBMITTER: Kuzmenkov AI 

PROVIDER: S-EPMC12334782 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature