# Scorpion Venom Neurotoxins: Molecular Diversity, Mechanisms, and Drug Scaffolds

## TL;DR

This review explores scorpion venom peptides, focusing on their molecular diversity, how they affect ion channels, and their potential for drug development.

## Contribution

The paper provides a comprehensive synthesis of current knowledge on scorpion venom neurotoxins and their therapeutic potential.

## Key findings

- Scorpion venom peptides modulate various ion channels, including Nav, Kv, Calcium, Chloride, and TRP channels.
- Omics and structural biology have expanded the catalog of venom peptides and their structure–function relationships.
- Scorpion venom peptides are promising leads for drug development due to their unique mechanisms of action.

## Abstract

Venom is a key evolutionary innovation of venomous organisms in the long-term process of survival adaptation. As one of the oldest arthropods, scorpions produce venom rich in bioactive peptides that also constitute a valuable pharmacological resource. Omics-driven discovery and structural biology have expanded the peptide catalog and clarified structure–function principles across disulfide-bridged (DBPs) and non-disulfide-bridged peptides (NDBPs). Within this arsenal, ion-channel targeting neurotoxins predominantly modulate Nav, Kv, Calcium, Chloride, and TRP channels to achieve predation, defense, and competition. Owing to their unique mechanisms of action and significant therapeutic potential, scorpion venom peptides have attracted sustained interest as leads and scaffolds for drug development. This review synthesizes current knowledge of scorpion venom composition, with an emphasis on the pivotal role of neurotoxins, covering their molecular diversity, structural features, and modes of ion-channel modulation, as well as emerging applications in disease treatment.