| Autor: |
Dias NB; Scientific and Technological Bioresource Nucleus (BIOREN-UFRO), Universidad de La Frontera (UFRO), Temuco 4811230, Chile., de Souza BM; Department of Basic and Applied Biology, Institute of Biosciences of Rio Claro, University of São Paulo State (UNESP), São Paulo 13506-900, Brazil., Cid-Alda F; Scientific and Technological Bioresource Nucleus (BIOREN-UFRO), Universidad de La Frontera (UFRO), Temuco 4811230, Chile., Dorce VAC; Butantan Institute, São Paulo 05503-000, Brazil., Cocchi FK; Department of Basic and Applied Biology, Institute of Biosciences of Rio Claro, University of São Paulo State (UNESP), São Paulo 13506-900, Brazil., Palma MS; Department of Basic and Applied Biology, Institute of Biosciences of Rio Claro, University of São Paulo State (UNESP), São Paulo 13506-900, Brazil. |
| Abstrakt: |
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. |
