Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens

Posted by
  Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens Abstract The venom of the slender black scorpion Centruroides nigrescens , from the State of Guerrero México, was fractionated by Sephadex G–50 gel filtration, followed by carboxymethyl cellulose ion separation and high–performance liquid chromatography, permitting to obtain two new peptides toxic to arthropods. The estimate LD 50 of the soluble venom for the insect Acheta domesticus was 11.1 μg/g body weight, and for the arthropod Armadillidium vulgare was 61.1 μg body weight . The amino acid sequence of toxin Cnige1 (toxic to A. domesticus and A. vulgare ) contains 65 amino acids, with a molecular mass of 7273.37 mass units, whereas toxin Cnige2, toxic to A. domesticus , contains 68 amino acids, with a molecular mass of 7548.81 units. Both peptides are well packed, containing 8 cysteines, which in the native venoms are forming 4 disulfide bridges each. The amino acid sequences f...

Targeting snake venom metalloproteinases: structural diversity, molecular pathogenesis and therapeutic interventions

Posted by

 


Targeting snake venom metalloproteinases: structural diversity, molecular pathogenesis and therapeutic interventions

Abstract

Snake venom Metalloproteinases (SVMPs) are Zn²⁺-dependent endopeptidases categorised under metzincin superfamily and are predominantly found in venom of the “Viperidae” family snakes. They are key mediators of venom-induced pathology with associated tissue damage including haemorrhage and oedema. SVMPs are classified as P-I, P-II, and P-III depending on the domains, each differing in structural complexity and organization. Further, the conserved HEXXHXXGXXH catalytic motif organizes a Zn2+ ion, essential for the breakdown of peptide bonds and proteins. Given the limitations of conventional antivenom therapy, increasing attention has been directed toward targeted approaches for SVMPs neutralization, including plant-derived phytocompounds, synthetic and repurposed small-molecule inhibitors, recombinant monoclonal antibodies, and camelid-derived nanobodies. Structure-based drug discovery, molecular docking, and mechanistic studies have facilitated the identification of compounds and biologics capable of interfering with SVMP catalytic activity, substrate recognition or functionally relevant epitopes. Emerging technologies such as CRISPR-engineered venom gland organoids and artificial intelligence/machine learning-assisted molecular screening further provide opportunities for functional target validation and rational therapeutic discovery. This review integrates these conventional and emerging strategies, highlighting the structural basis of SVMPs inhibition and their potential to support the development of precise, broad-spectrum, and next-generation therapeutic interventions against SVMP-mediated envenoming.

Dodakallanavar, J., Harish, D.R., Hiremath, K. et al. Targeting snake venom metalloproteinases: structural diversity, molecular pathogenesis and therapeutic interventions. Mol Biol Rep 53, 1619 (2026). https://doi.org/10.1007/s11033-026-12781-z