The biology

Why arthropod venom peptides?

Because a venom is not a poison. It is a purpose-built pharmacology library, refined by selection pressure that punishes every wasted residue.

Evolutionary precision

400+ million years of optimization

  • Natural selection has optimized venom peptides to hit specific ion channels with nanomolar affinity.
  • Evolution solved the selectivity problem that medicinal chemistry has not.
  • Ion channel hit rates from venom libraries far exceed small-molecule screening campaigns.
Structural novelty

Chemistry no small molecule occupies

  • Cysteine-rich ICK (inhibitor cystine knot) folds, short cysteine-free peptides, and disulfide-stabilized scaffolds are structurally distinct from every approved small molecule.
  • That distinctness enables IP protection and escape from existing resistance mechanisms.
  • The ICK fold is intrinsically protease-resistant, so stability comes built in.
Ion channels

Selectivity is the whole game

  • Small molecules modulate ion channels but lack specificity, because the subtypes are too similar to each other.
  • Convergence validation: four different Sonoran arthropod peptide families selectively modulate ion channels.
Why convergence matters. When four structurally unrelated peptide families, evolved independently in four separate lineages, all arrive at the same human drug targets, the result is not a coincidence to be explained away. It is replication, run four times, by an experimenter with 400 million years and no publication bias.