Cicileus derradji sp. nov., a new species from southern Algeria (Scorpiones: Buthidae)

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  Cicileus derradji sp. nov., a new species from southern Algeria (Scorpiones: Buthidae) Abstract A new scorpion species, Cicileus derradji sp. nov., is described from Tin Zaouatine District, In Guezzam Province, southern Algeria. The description is based on an adult male holotype, an adult female paratype and a juvenile specimen, and is supported by detailed morphological analyses, including colouration, morphometrics, carination patterns and trichobothrial arrangement. This discovery extends the known distribution of the genus Cicileus approximately 500 km southwestward within Algeria. With the addition of this species, the number of recognised species in the genus increases to six. The new species is compared with all previously known species of Cicileus , and detailed colour photographs, including images taken under ultraviolet illumination, are provided. Derradj, L., Aydın Yağmur, E., Benali, N., & Bikada, M. (2026). Cicileus derradji sp. nov., a new species from south...

Design of antinociceptive peptide by grafting domains between scorpion β-neurotoxins

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Design of antinociceptive peptide by grafting domains between scorpion β-neurotoxins

Abstract

Neurotoxic peptides from venomous animals have been pointed out as antinociceptive therapeutic leads. Venom peptides have modulation properties on isoforms of voltage-gated sodium channels (VGSC), associated with pathologies such as neuropathic or inflammatory pain. The β-neurotoxins obtained from scorpion venoms are peptides that can alter the kinetics of VGSC by binding to its receptor site 4. CeII8 is a non-lethal scorpion β-neurotoxin that has been reported to interact with hNaV1.7, a VGSC isoform related to the codification and processing of painful stimulus (nociception), and it is involved in pain pathologies. On the other hand, CssII is a lethal scorpion β-neurotoxin that binds mainly to site 4 of hNav1.6. Because of this, we used computational methods and the amino acid sequence of the novo recombinant neurotoxin rCssII-RCR to graft in some of its domains existing amino acids from the non-lethal CeII8 to generate a chimeric peptide with antinociceptive activity, named rCssII-Del-D23A-TCD. This peptide variant was found to have antinociceptive activity in inflammatory and neuropathic pain models with an effect comparable to the mu-opioid receptor agonists DAMGO (H-Tyr-D-Ala-Gly-N(Me) Phe-Gly-ol).
Montero-Dominguez, P. A., Restano-Cassulini, R., Magaña-Ávila, L. C., Almanza, A., Mercado, F., & Corzo, G. (2025). Design of antinociceptive peptide by grafting domains between scorpion β-neurotoxins. Bioorganic Chemistry, 162, 108592. https://doi.org/10.1016/j.bioorg.2025.108592