An integrative description of Euscorpius diagorasi sp. n. from Rhodes, Greece (Scorpiones: Euscorpiidae)

  An integrative description of Euscorpius diagorasi sp. n. from Rhodes, Greece (Scorpiones: Euscorpiidae) Abstract The genus  Euscorpius  Thorell, 1876 comprises a diverse and taxonomically challenging group of scorpions in the Mediterranean, with Greece representing one of its principal centers of diversity. In this study, we provide an integrative description of  Euscorpius diagorasi   sp. n. , a new species from Rhodes Island, Greece. The new species is described on the basis of adult male and female morphology and mitochondrial COI sequence data. It is a small oligotrichous species characterized by a total length of approximately 21–25 mm, pale yellow to light brown coloration with darker reddish-brown pedipalps, pectinal tooth count of 8 in the male and 7 in the females, Pv = 7–8, Pe-et = 5–6, and a distinct mitochondrial lineage. Phylogenetic analyses based on COI recovered the Rhodian specimens as a strongly supported monophyletic lineage, sister to...

Profiling the Linear Peptides of Venom from the Brazilian Scorpion Tityus serrulatus: Structural and Functional Characterization

 


Profiling the Linear Peptides of Venom from the Brazilian Scorpion Tityus serrulatus: Structural and Functional Characterization

Abstract

Scorpion venoms are a rich source of bioactive peptides, most of which are neurotoxic, with 30 to 70 amino acid residues in their sequences. There are a scarcity of reports in the literature concerning the short linear peptides found in scorpion venoms. This type of peptide toxin may be selectively extracted from the venom using 50% (v/v) acetonitrile. The use of LC-MS and MS/MS enabled the detection of 12 bioactive short linear peptides, of which six were identified as cryptides. These peptides were shown to be multifunctional, causing hemolysis, mast cell degranulation and lysis, edema, pain, and anxiety, increasing the complexity of the envenomation mechanism. Apparently, the natural functions of these peptide toxins are to induce inflammation and discomfort in the victims of scorpion stings.

Profiling the Linear Peptides of Venom from the Brazilian Scorpion Tityus serrulatus: Structural and Functional Characterization, Nathalia Baptista Dias, Bibiana Monson de Souza, Fernanda Cid-Alda, Valquíria Abrão Coronado Dorce, Fernando Kamimura Cocchi, and Mario Sergio Palma, Journal of Natural Products Article ASAP
DOI: 10.1021/acs.jnatprod.3c01085