| Texto completo | |
| Autor(es): |
dos Santos, Roney Vander
[1]
;
Grillo, Giovanna
[1]
;
Fonseca, Henrique
[1]
;
Stanisic, Danijela
[1]
;
Tasic, Ljubica
[1]
Número total de Autores: 5
|
| Afiliação do(s) autor(es): | [1] Univ Estadual Campinas, Inst Chem, Organ Chem Dept, Biol Chem Lab, UNICAMP, Campinas, SP - Brazil
Número total de Afiliações: 1
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Toxicon; v. 198, p. 64-72, JUL 30 2021. |
| Citações Web of Science: | 0 |
| Resumo | |
The majority (90%) of the snakebite envenomation in Brazil accounts for Bothrops from the Viperidae family. Some snake venom serine proteases provoke blood coagulation in ophidian accident victims because of their fibrinolytic activity, one of those proteases from Bothrops jararaca (B. jararaca) has been chosen for this study. Our objectives were to isolate and characterize the target serine protease; isolate, purify, and characterize the orange bagasse flavone (hesperetin, Hst), and investigate the interactions between the targets, enzyme, and hesperetin. The purified serine protease was named BjSP24 because of its molecular mass and proteolytic activity. BjSP24 was folded and characterized using circular dichroism and showed low alpha-helix contents (7.7%). BjSP24 exhibited sequence similarity to other known snake venom serine proteases as measured in the enzyme tryptic peptides' LC-MS/MS run. Hesperetin was obtained within the expected yield and with the predominance of 2S isomer (82%). It acted as a mixed inhibitor for the serine protease (SVSP) from Bothrops jararaca snake venom observed in three different in vitro experiments, fluorescence, kinetics, and SSTD-NMR. It is still to determine if hesperetin might aid-in reverting the on site blood clotting problems just after snakebite accidents. (AU) | |
| Processo FAPESP: | 16/21682-0 - Estudos bioquímicos de uma serina protease de peçonha de serpente |
| Beneficiário: | Giovanna Rivabem Grillo |
| Modalidade de apoio: | Bolsas no Brasil - Iniciação Científica |