Avaliação da atividade anticoagulante e bloqueadora de elastase de um inibidor de tripsina isolado de Caesalpinea pyramidalis Tul.
Plants are subject to a diversity of unfavorable biotic and abiotic conditions, undergoing constantly some evolutionary adaptation, that can contribute to its reproduction and survival. The development of sophisticated defense strategies against pests and pathogens such as the synthesis of several n...
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| Formato: | Dissertação |
| Idioma: | pt_BR |
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Universidade Federal do Rio Grande do Norte
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| Endereço do item: | https://repositorio.ufrn.br/handle/123456789/45819 |
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| Resumo: | Plants are subject to a diversity of unfavorable biotic and abiotic conditions,
undergoing constantly some evolutionary adaptation, that can contribute to its reproduction
and survival. The development of sophisticated defense strategies against pests and
pathogens such as the synthesis of several natural bioactive compounds stands out as
part of this adaptive biological arsenal. A key group of bioactive molecules in this context
are the protease inhibitors, which compromise the activity of digestive enzymes of
herbivores, as well as an action of pathogens, contributing to the balance of biological
interactions. Protease inhibitors, are important molecules because of their heterologous
potential in other biological systems, and may have in vitro and in vivo effects on several
biological models, as well as therapeutic properties in a range of disorders that
compromise human health. In this work an inhibitor of serinoprotease (CpTI), was isolated
from the Caesalpinia pyramidalis Tul. seeds by fractionation of the crude extract with 30-
60% ammonium sulfate, followed by separation in affinity chromatography on TrypsinSepharose 4B-CNBr-actived column, the retained peak was enriched in inhibitory activity
for trypsin, chymotrypsin and elastase serine protease type. The thermostability test
showed that CpTI was able to maintain its functionality up to 80 °C and the concentrations
required to inhibit 50% of the activity of the trypsin, human neutrophil elastase and
chymotrypsin enzymes were 17, 21 and 156 μg/mL, respectively. CpTI also prolonged the
coagulation time by the intrinsic pathway (TPPa) in more than 80 seconds at a
concentration of 36.2 μg / mL. It was also observed that CpTI has no cytotoxic activity to
red blood cells at any of the concentrations tested (0,03 , 0,125 e 0,5 mg/mL). These
results demonstrate the potential therapeutic use of CpTI in processes involving
inflammation and coagulation. |
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