NMR in interaction studies of a serine protease from snake venom
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Palavras-chave

Enzymes
Inhibitors
NMR

Como Citar

GRILLO, Giovanna; TASIC, Ljubica; SANTOS, Roney dos. NMR in interaction studies of a serine protease from snake venom. Revista dos Trabalhos de Iniciação Científica da UNICAMP, Campinas, SP, n. 27, p. 1–1, 2019. DOI: 10.20396/revpibic2720192080. Disponível em: https://econtents.sbu.unicamp.br/eventos/index.php/pibic/article/view/2080. Acesso em: 15 mar. 2026.

Resumo

In this research, we have purified a serine protease from Bothrops jararaca venom (BjSP24). This enzyme showed molar mass of 24.4 kDa as determined using MALDI-TOF. BjSP24 inhibition by hesperitin (Hst) was studied using florescence, enzymatic kinetics and nuclear magnetic resonance techinique (Saturation Transferee Difference, STD-NMR).

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Referências

R. Vander dos Santos, F. Villalta-Romero, D. Stanisic, L. Borro, G. Neshich e L. Tasic, Toxicon 2018, 143, 36 – 43.

F. V. Romero, L. Borro, B. Mandic, T. Escalante, A. Rucavado, J. M. Gutiérrez, G. Neshich e L. Tasic, Bioorganic & Medical Chemistry Letters 2017, 27, 2018-2011.

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