Caracterização bioquímica parcial dos componentes presentes na peçonha bruta da formiga Odontomachus chelifer

• Autor(a) principal: Damorin, Tulio Morato
• Data de Publicação: 2019
• Tipo de documento: Trabalho de conclusão de curso
• Idioma: por
• Título da fonte: Repositório Institucional da UFU
• Texto Completo: https://repositorio.ufu.br/handle/123456789/36172
• topic: Odontomachus chelifer; Odontomachus chelifer; Peçonha bruta; Gross venom; Caracterização bioquímica; Biochemical; Enzimática; Enzymatic and functional characterization; Funcional; CNPQ::CIENCIAS BIOLOGICAS

Ants are insects of the Formicidae family presenting a widely diversified taxonomic group represented by 20 families among which 16 are provided with stingers and thus classified as venomous. The major function of these 16 subfamilies venom is multifold, there being highlighted self-defense against predators, capture of preys and social communication; the venom comprises a mixture of carbohydrates, formic acid, bioactive amines, free amino acids, alkaloids, proteins and peptides. Approximately 70% of the dry weight of an ant venom is peptides and these have molecular mass varying between 1.4 and 7 kDa and are among the allergens of the venom; among the proteins there can be highlighted phospholipases, hyaluronidases and serinoproteases. On the whole, the compounds present in the venom of an ant can be harmful to the human body. However, scientific studies have shown that isolated compounds can point to a variety of pharmacological properties among which those of antitumorous action, hemolytic, antimicrobial, anti-inflammatory, anaesthetic, neuroactive and anticonvulsive. This work has proposed a biochemical, enzymatic and functional study of the gross venom of O. chelifer. Among the innumerable species of ant of the Odontomachus genus, the species O. chelifer is a promising choice for scientific researches owing to its venom having scarcely been studied and there being little or no information on this species in the literature. The electrophoretic analysis (SDS-PAGE) of the gross venom of the O. chelifer showed a proteic profile with a large number of compounds whose molar masses varied from 14 to 97 kDa when analysed under reducing conditions, with a more intense marking for bands around 97, 50, 40, 25 kDa and under 14.4 kDa. There was no positive result for the phospholipase A2 active test, the assumption for that being the fact that the species O. chelifer does not present enzymes of the phospholipase A2 class in its venom. The assessment of the regulating activity showed the gross venom of O. chelifer not capable of coagulating the citrated bovine plasma, different from the positive control, the B. Pauloensis venom, which coagulated the plasma in 18.2 seconds. In short, it was possible to identify toxins over a wide range of molar masses, there being necessary, however, new studies in order to identify compounds with enzymatic and biological actions in the gross venom of the O. chelifer ant.