Venoms are mixtures of small, tightly folded peptides that evolved to hit nerve and muscle targets fast. Several drugs started there. Exenatide, the first GLP-1 drug, came from a peptide in Gila monster saliva, and ziconotide (Prialt), a pain drug infused into the spine, is a copy of a cone snail toxin.
Scorpion venoms are a rich source of peptides that block ion channels, the pores that control nerve signals. A 2026 review in Frontiers in Pharmacology counted 176 neuropeptides from 107 scorpion species. Selectivity in a dish does not always carry over, though: in October 2026, a University of Tübingen team found that BMK86-P1, a scorpion-toxin peptide that blocks one potassium channel, had little effect in mouse neurons, where that channel usually pairs with another.
Newer work uses venom shapes as starting points for design. A 2026 study built a library from about 482 venom-derived scaffolds and, with machine learning and phage display, found binders for all four drug targets it tested.
See #ion-channels, #antimicrobial-peptides, and #ai-drug-design.
Researchers at the Hebrew University of Jerusalem designed melittin derivatives and ran experimental evolution tests in Staphylococcus aureus: full-length melittin and highly hydrophobic variants drew high resistance, while the truncated Mel(5-24) kept its antibacterial activity with minimal resistance and less cross-resistance to other peptides. Melittin-evolved bacteria shared mutations in pmtR, while Mel(5-24)-evolved bacteria changed only ydbT, and resistance tracked with peptide hydrophobicity and length, the Antimicrobial Agents and Chemotherapy paper reports. The work was done in lab cultures.
Researchers at Rzeszów University of Technology, with colleagues in Gdańsk, Kraków, and Ljubljana, built AMPAB5 from cobra (Naja ashei) venom factor sequences. Against Pseudomonas aeruginosa, which resists chloramphenicol (MIC 250 μg/mL), combining the two cut the MICs to 15.63 μg/mL for the antibiotic and 5.86 μg/mL for the peptide; AMPAB5 also blocked and cleared biofilms, modulated IL-1β and TNF-α release by human macrophages, and showed no hemolysis or toxicity to skin or Caco-2 cells, the Toxicology and Applied Pharmacology paper reports. The work was done in cells only, and two authors hold a patent assigned to the university.
Researchers at Hubei University of Technology, Hubei University of Medicine, and partner institutions in China reported in Microbiology Spectrum on October 28, 2026 that BmKDfsin3, a scorpion venom peptide, reduced replication of severe fever with thrombocytopenia syndrome virus (an RNA virus) and herpes simplex virus type 1 (a DNA virus) in human lung cells, mainly after the viruses entered. The peptide blocked the viruses' activation of the p38 pathway and strengthened type I and III interferon responses. It showed low toxicity to cells, red blood cells, and mice; antiviral effects have not been tested in animals or people.
Researchers at the University of Liège and Alphabiotoxine Laboratory in Belgium reported in Frontiers in Chemistry on October 27, 2026 a workflow that captures venom peptides on native membrane preparations carrying a target receptor, then identifies them by MALDI-TOF and LC-MS/MS. Tested on the human vasopressin V2 receptor and the muscle-type nicotinic acetylcholine receptor, it recovered known ligands, including endogenous peptides and disulfide-rich venom toxins, and flagged additional toxins preferentially bound by nicotinic receptor-rich Torpedo membranes for follow-up. The authors say the method can be adapted to other membrane receptors and peptide libraries.
Researchers at Brazil's State University of Campinas (UNICAMP) reported in Immunology on October 25, 2026 that LW-9, a peptide isolated from the venom of the Brazilian wandering spider Phoneutria nigriventer, delayed tumor growth in mice with EO771 breast tumors, with a stronger effect combined with the chemotherapy drug doxorubicin. At 1 µg/kg it caused no significant changes in liver or kidney markers, and mice given it with doxorubicin ate more and held their weight better than mice on doxorubicin alone. Tumors in the combination group had less PD-L1 and more T cells, including GITR-positive T cells; the work is in mice.
Researchers at Hainan Medical University reported in Molecules on October 23, 2026 a new peptide, Ed-79, found by screening the transcriptome of the sea anemone Exaiptasia diaphana: 37 amino acids held together by three disulfide bonds, made by solid-phase synthesis and folded in three oxidative steps. It killed fall armyworm (Spodoptera frugiperda) and mealworm (Tenebrio molitor) larvae in a dose-dependent way, with LD50 values of 289.5 and 367.2 pmol/g. Computer docking predicts it binds the outer vestibule of the Shaker potassium channel; that binding mode has not been confirmed experimentally.
Researchers at Hubei University of Medicine reported in Biomolecules on October 19, 2026 that SjAPI-2, a small peptide from scorpion venom, inhibited the classical complement pathway, part of the immune system that can damage the body's own tissue, by binding the complement proteins C4 and C4b. Mapping showed a loop between residues K30 and V38 does the work, and the peptide limited heart muscle damage in an ischemia-reperfusion injury model. The authors describe it as the first anti-complement peptide reported from scorpions; the work is preclinical.
Neurologists at the University of Tübingen's Hertie Institute reported in Frontiers in Pharmacology on October 13, 2026 that BMK86-P1, a synthetic scorpion-toxin peptide, selectively blocked Kv1.2 potassium channels made only of Kv1.2 units in cells but barely affected channels mixed with Kv1.1, the form common in the brain. In mouse neurons it produced little change in firing or synaptic activity. The authors, who study gene variants in these channels that cause epilepsy, said the work shows the limits of using such toxins as precise research tools.
A venom-peptide discovery system published in Pharmaceuticals (MDPI) in 2026 paired phage display with a machine-learning model that predicts mutation-tolerant residues, building a library from roughly 482 venom-derived scaffolds. Screened against CD47, DLL3, IL33, and P2X7R, the resulting VCX library yielded strong binders for all four targets. Venom peptides are stabilized by multiple disulfide bonds and naturally evolved to hit GPCRs and ion channels, giving them structural stability that conventional peptides often lack.
A Frontiers in Pharmacology review cataloged 176 neuropeptides across 16 families found in the venoms of 107 scorpion species, highlighting Buthus martensii Karsch (BmK) peptides as selective ion channel modulators. Examples include MarTX (selective for BK(α+β4) channels) and BmKTX (Kv1.3 blocker) — positioning scorpion venom as an underexplored source of next-generation neurotherapeutic leads for pain, epilepsy, and autoimmune conditions.