Venomics of the six-eyed sand spider, Sicarius rugosus (Araneae: Sicariidae), from the neotropical dry forest of Costa Rica

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  Venomics of the six-eyed sand spider, Sicarius rugosus (Araneae: Sicariidae), from the neotropical dry forest of Costa Rica Abstract Background Sicarius rugosus , the only member of the genus that inhabits Central America, is phylogenetically related to South American  Sicarius  spiders. These originated from a common ancestor with sister African species. Like  Loxosceles ,  Sicarius  exhibits venom phospholipase D activity due to a group of toxins known collectively as SicTox. Methods A gel-assisted, bottom-up, proteomic analysis was performed to characterize the venom composition of  S. rugosus . Hyaluronidase activity was determined using zymography. Results We identified several SicTox sequences, all classified as β-clade paralogs and sharing unique peptides with proteins from  S. patagonicus ,  S. peruensis,  and other species. Enzymes such as metalloproteinases, including putative astacins, carboxypeptidases, and angiotensin-conv...

Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential

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Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential

Abstract

Scorpion venom is a rich source of bioactive compounds with significant potential for anticancer drug development. Its diverse molecular composition, including neurotoxins, antimicrobial peptides, and enzymes, provides a vast library for therapeutic innovation. Proteomic analyses have characterized venom composition in several species, while further functional assays have clarified their anticancer mechanisms. This review synthesizes current knowledge on scorpion venom-derived peptides with demonstrated anticancer activity, which selectively target ion channels, induce apoptosis, or disrupt tumor microenvironments. Where available, we highlight proteomic studies that have identified these components and discuss their structural features relevant to drug design. We also examine clinical applications and the challenges in translating venom peptides into therapies. The crucial and growing role of proteomics in this field, particularly for venom fractionation, component identification, and structural characterization, is critically evaluated.