Banca de QUALIFICAÇÃO: JOELTON IGOR OLIVEIRA DA CRUZ

Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.
DISCENTE : JOELTON IGOR OLIVEIRA DA CRUZ
DATA : 31/08/2017
HORA: 08:30
LOCAL: Sala da Pós-Graduação
TÍTULO:

ISOLATION AND PARTIAL CHARACTERIZATION OF A SERINOPROTEASE INHIBITOR OF Caesalpinea pyramidalis Tul.: ANTICOAGULANT AND INHIBITOR PROPERTIES OF ELASTASE.

PALAVRAS-CHAVES:

Catingueira; trypsin inhibitor, human neutrophilic elastase; coagulation

PÁGINAS: 60
GRANDE ÁREA: Ciências Biológicas
ÁREA: Bioquímica
SUBÁREA: Química de Macromoléculas
ESPECIALIDADE: Proteínas
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 and pathogens, contributing to the balance of biological interactions. Protease inhibitors, are important molecules because of their heterologous potential in other biological systems, may have an in vitro and in vivo effects on various pathogen models, as well as therapeutic properties in a range of disorders that compromise human health. In this work an inhibitor of serinoprotease (CpSPI), 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 Trypsin-Sepharose 4B column, the retained peak was enriched in inhibitory activity for trypsin, chymotrypsin and elastase serine protease type. The thermostability test showed that CpSPI 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. CpSPI also prolonged the coagulation time by the intrinsic pathway (TPPa) in more than 120 seconds at a concentration of 36.2 μg / mL. It was also observed that CpSPI has no cytotoxic activity to peripheral blood red blood cells at any of the concentrations tested (0,03 , 0,125 e 0,5 mg/mL). These results demonstrate the potential immunomodulatory and anticoagulant therapeutic use of CpSPI.

MEMBROS DA BANCA:
Presidente - 1549705 - ADRIANA FERREIRA UCHOA
Interno - 2985070 - JONAS IVAN NOBRE OLIVEIRA
Externo à Instituição - PAULA IVANI MEDEIROS DOS SANTOS - IFRN