AaTs-1, a Tetrapeptide from Scorpion Venom Mitigates Demyelination and Neuroinflammation in a Cuprizone-Induced Model of Multiple Sclerosis

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  AaTs-1, a Tetrapeptide from Scorpion Venom Mitigates Demyelination and Neuroinflammation in a Cuprizone-Induced Model of Multiple Sclerosis Abstract Purpose This study focuses on the evaluation of the therapeutic potential of Tetrascorpin-1 (AaTs-1), a tetrapeptide isolated from Androctonus australis hector venom, proposed as a putative formyl peptide receptor 2 (FPR2) antagonist, in a cuprizone-induced murine model of Multiple sclerosis (MS), a chronic autoimmune and inflammatory disease of the central nervous system. Methods Acute demyelination was induced in mice by administering cuprizone (0.2% w/w in the diet) for six weeks. During the sixth week of cuprizone intake, demyelinated mice received intranasal administration of AaTs-1 at a dose of 50–100 µg/kg for five consecutive days, with 24-hour intervals between treatments. Results Behavioral assessments, immunological assays, and histological analyses revealed that AaTs-1 improved body weight, reduced behavioral impairments...

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