Advancing the systematics of Araneae: ultraconserved elements phylogenomics demonstrates the non-monophyly of Miturgidae Simon, 1886 and supports the Familial Rank of Systariidae Deeleman-Reinhold, 2001

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  Advancing the systematics of Araneae: ultraconserved elements phylogenomics demonstrates the non-monophyly of Miturgidae Simon, 1886 and supports the Familial Rank of Systariidae Deeleman-Reinhold, 2001 Abstract The systematic status of the family Miturgidae Simon, 1886 and related subfamilies has long been problematic, primarily due to challenges in interpreting morphological characters and limited molecular sampling. In this study, we reconstruct the phylogeny of Miturgidae using ultraconserved elements and estimate its divergence time. Our results suggest that Systariinae does not belong to Miturgidae, but rather is sister to all other families of the Dionycha B clade. Consequently, we elevate it to family rank as Systariidae Deeleman-Reinhold, 2001 and discuss its morphological synapomorphies. Furthermore, our analyses place Miturgidae as the sister clade to Viridasiidae + Selenopidae under multiple phylogenetic methods. Divergence time estimates indicate an ancient origin of...

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