AI Article Synopsis
- Scorpion venoms contain bioactive peptides primarily made up of 30 to 70 amino acids, with many being neurotoxic.
- Research has identified 12 short linear peptides from scorpion venom, six of which are classified as cryptides, using techniques like LC-MS and MS/MS.
- These peptides have multiple functions, including causing hemolysis, pain, and inflammation, which complicates the process of envenomation for the victim.
Article 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.
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| http://dx.doi.org/10.1021/acs.jnatprod.3c01085 | DOI Listing |
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