Venom Mass Fingerprints for Species Delimitation, Reloaded: A Test Case with Italian Scorpions (Euscorpius)

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  Venom Mass Fingerprints for Species Delimitation, Reloaded: A Test Case with Italian Scorpions (Euscorpius) Abstract Scorpion venoms are complex mixtures of bioactive compounds including proteins, peptides and enzymes. Although venoms exhibit substantial intraspecific variation, some compounds appear to be species-specific, highlighting their potential as chemotaxonomic markers. Venom mass fingerprints (MFPs) derived from Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-TOF) Mass Spectrometry (MS) have been proposed as a means of delimiting species. However, their utility for species delimitation has rarely been evaluated against independent sources of taxonomic evidence. In the present study, the performance of MALDI-TOF MS-based venom peptide barcoding (mass ranges of m/z 800‒4500 and m/z 3000‒10,000) was assessed in 52 populations of eight Italian species of the scorpion genus Euscorpius Thorell, 1876, representing different levels of evolutionary divergenc...

Scorpion Venom Peptides: From Structural Scaffolds to Therapeutic Applications—A Focus on Antioxidant Mechanisms and Translational Perspectives

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Scorpion Venom Peptides: From Structural Scaffolds to Therapeutic Applications—A Focus on Antioxidant Mechanisms and Translational Perspectives

Abstract

Scorpion venom peptides, with their stable disulfide backbone, compact structural framework, and highly selective regulation of ion channels, have long been regarded as important molecular probes in neuropharmacology. However, recent studies have revealed their potential for regulating oxidative stress, inflammation, and neuroprotection, making them a new research frontier. In this article, we focus on scorpion venom peptides as drugs, constructing an integrated knowledge framework from structural classification to clinical translation. First, scorpion venom peptides are systematically classified based on cysteine arrangement patterns and three-dimensional folding topology, and their structure–activity relationships are summarized. Based on this, the molecular mechanisms by which scorpion venom peptides regulate ion channels are systematically analyzed. We review the emerging pharmacological activities of scorpion venom peptides. Of particular note, the representative molecule SVHRSP has shown multi-target synergistic antioxidant and neuroprotective activity in models of Parkinson’s disease. We also systematically evaluate the application of engineering strategies, including cyclisation modification, nanodelivery, recombinant expression, and AI-assisted optimization, to overcome the translational bottlenecks in the development of scorpion venom peptides. However, it should be noted that most SVHRSP-related findings have been reported by a single research group; independent replication, pharmacokinetic characterization, and human efficacy data are still lacking. Its IND approval permits clinical investigation but does not yet constitute proven therapeutic benefit in patients. By integrating molecular structure, redox regulation mechanisms, and translational medicine perspectives, this review aims at providing a theoretical basis and practical pathways for scorpion venom peptides as precision therapeutic molecules for oxidative stress-related diseases. 

Wang, M., Li, H., Li, S., Guo, Y., Xu, Y., Zhao, J., & Chen, L. (2026). Scorpion Venom Peptides: From Structural Scaffolds to Therapeutic Applications—A Focus on Antioxidant Mechanisms and Translational Perspectives. Antioxidants. https://doi.org/10.3390/antiox15060747