Drug intelligence / Profile preview

scorpine

Development stage: Preclinical
Modality: Peptides

Overview

Scorpine is a multifunctional cationic peptide originally isolated from the venom of the emperor scorpion (*Pandinus imperator*). It belongs to the beta-KTx or scorpine-like peptide family, characterized by a unique dual-domain structure: an N-terminal amphipathic alpha-helix with cytolytic and antimicrobial activity (resembling cecropins), and a C-terminal domain containing a cysteine-stabilized alpha/beta (CS-αβ) motif with potassium channel-blocking activity (resembling defensins). Scorpine exhibits potent antibacterial, antimalarial, and antiviral activities, and has been shown to inhibit the development of *Plasmodium berghei* and *Plasmodium falciparum* parasites. It is being investigated for potential therapeutic applications in infectious diseases and as a paratransgenetic tool in mosquitoes to control malaria transmission.

Other names: scorpin

Targets

Kir (Inward-rectifier potassium channels)

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