Scorpion Venom Peptides: Novel Therapeutic Approaches for Inflammatory and Hepatic Disorders

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  Scorpion Venom Peptides: Novel Therapeutic Approaches for Inflammatory and Hepatic Disorders Abstract Chronic hepatic disorders, such as metabolic dysfunction associated steatohepatitis (MASH), alcohol associated liver disease (ALD), and viral hepatitis (Hepatitis B Virus [HBV]/Hepatitis C Virus [HCV]), are primarily driven by persistent immune-mediated inflammation and hepatic stellate cell activation leading to fibrosis, yet conventional therapies lack tissue and molecular specificity. Scorpion venom peptides, refined through evolutionary selection, provide highly potent, target specific scaffolds capable of modulating intrahepatic inflammatory networks. Recent in vivo preclinical studies indicate that voltage gated potassium (Kv1.3) channel blocking peptides, such as BmKK2, significantly reduce macrophage activation and inhibit downstream cytokine production, effectively ameliorating diet-induced steatohepatitis and tissue scarring in murine models. Engineered hepatotropic ca...

Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities

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Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities

Abstract

Spider venoms are primarily composed of small neurotoxic peptides. However, recent studies suggested a hitherto overlooked diversity of spider venom enzymes, although their functional space still remains largely unexplored. We tested 10 spider venoms for enzymatic activities covering six enzyme classes and found that all tested enzymatic activities can be detected in at least some of the venoms and that hyaluronidases exhibit particularly high enzymatic activities. With this, our study provides functional evidence for the proposed biological significance of enzymes in spider venoms, but more detailed investigations are required.
Dresler, J., Herzig, V., Schulte, L., & Lüddecke, T. (2025). Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities. Toxicon, 108667. https://doi.org/10.1016/j.toxicon.2025.108667