In Memoriam: Giraldo Alayón García

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  In Memoriam: Giraldo Alayón García -  Photo © Facebook/National Museum of Natural History of Cuba In Memoriam: Giraldo Alayón García The arachnological community mourns the loss of Giraldo Alayón García, a Cuban zoologist whose work helped bring the spiders of Cuba and the wider Caribbean into clearer scientific view. As a researcher and curator at Cuba’s National Museum of Natural History, Dr. Alayón devoted decades to studying arachnids. His publications on spider taxonomy, evolution, and biogeography gave other researchers a stronger foundation for understanding the region’s biodiversity. He also shared that knowledge through teaching and scientific exchange far beyond Cuba. For those of us who care about taxonomy, his legacy is a reminder of the patient work behind every species description: examining specimens, recording differences, and preserving knowledge that others can build upon. His contributions will continue to guide the study of Caribbean spiders for years to ...

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