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...

Synthesis of U-theraphotoxin-Pv1a_1, an Aedes aegypti larvicidal disulfide bridged peptide from the Colombian tarantula Pamphobeteus verdolaga (Araneae: Theraphosidae)

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Synthesis of U-theraphotoxin-Pv1a_1, an Aedes aegypti larvicidal disulfide bridged peptide from the Colombian tarantula Pamphobeteus verdolaga (Araneae: Theraphosidae)

ABSTRACT

The attention to the increased resistance of Aedes aegipty to traditional insecticides has been directed to the development of bioinsecticides, such as those produced by insect predators, e.g. spiders. Here we present the solid-phase synthesis of native U-theraphotoxin-Pv1a_1 (n-Pv1a_1) from Pamphobeteus verdolaga, an active (by contact) insecticidal peptide against A. aegipty. U-theraphotoxin-Pv1a_1 sequence was gathered from venom proteomics and venom gland transcriptomics of Pamphobeteus verdolaga, and synthesized by solid phase using the Fmoc strategy followed by dimethyl sulfoxide promoted native disulfide bond formation. The synthetic peptide (s-Pv1a_1) was assayed for larvicidal activity in II and III instar A. aegypti larvae, as well as for cytotoxicity in human red blood and HaCat cells. s-Pv1a_1 showed potent activity towards A. aegypti larvae in the micro molar range, while showing no hemolytic activity and mild cytotoxicity to HaCat cells. Its potent contact activity makes n-Pv1a_1 and its synthetic version, s-Pv1a, promising biopesticides for the control of mosquito populations.

Estrada-Gómez, S., Salinas-Restrepo, C., Vargas Muñoz, L. J., Guzmán, F., Latorre, C. S., Pla, D., Sanz, L., & Calvete, J. (2025). Synthesis of U-theraphotoxin-Pv1a_1, an Aedes aegypti larvicidal disulfide bridged peptide from the Colombian tarantula Pamphobeteus verdolaga (Araneae: Theraphosidae). Toxicon: X, 100224. https://doi.org/10.1016/j.toxcx.2025.100224