PEPTIDOMIC CHARACTERIZATION OF THE VENOM FROM
Transcrição
PEPTIDOMIC CHARACTERIZATION OF THE VENOM FROM
PEPTIDOMIC CHARACTERIZATION OF THE VENOM FROM THE COLOMBIAN SCORPION Centruroides margaritatus Guerrero-Vargas, J.A .1,2, Fontes, W.1, Sousa, M.V.1, Castro, M.S.1,3 1 Centro Brasileiro de Serviços e Pesquisas em Proteínas, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília/DF, Brasil; 2 Grupo de Investigaciones Herpetológicas y Toxinológicas, Universidad del Cauca, Popayán, Colombia; 3Laboratório de Toxinologia Instituto de Ciências Biológicas, Universidade de Brasília/DF, Brasil Scorpion venoms are a complex mixture of peptides that exert their action via ion-channel modulation in biological membranes. In the present report we describe the first peptidomic characterization of the venom from the Colombian scorpion Centruroides margaritatus. This species is capable of producing moderate accidents and serious complications in humans, but little information is available related to its components. The crude venom was fractioned by RP-HPLC using a C8 column (4.6 x 250 mm) and 43 fractions were collected and vacuum dried. All these fractions were analyzed by MALDI-TOF MS and 91 distinct compounds had their molecular masses characterized. The venom of C. margaritatus exhibits 54% of their toxins in the molecular mass range from 2.5 to 6.0 kDa that probably includes short-chain K+ channel blockers; 13% of the total are in the range from 6.5 to 8.0 kDa and may include long-chain Na + channel toxins. Finally, 33% of the components present in C. margaritatus venom are peptides smaller than 2.0 KDa, a group rarely described in scorpions venoms. Two purified peptides with molecular masses of 2.6 kDa and 3.3 kDa were sequenced using automated Edman degradation. The first toxin was called MgTx2 and exhibits similarities to other scorpions K+-blocking neurotoxins, and the second peptide was called MgTx3 and no significant sequence similarity to other neurotoxins was detected. KEYWORDS Scorpion, Centruroides margaritatus, Colombia, MALDI-TOF/MS, Peptidomic characterization, Edman degradation. Support: FUB/UnB and CAPES
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