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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
20/07/2018 |
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Data da última atualização: |
07/01/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SANTOS, R. V. dos; VILLALTA-ROMERO, F.; STANISIC, D.; BORRO, L.; NESHICH, G.; TASIC, L. |
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Afiliação: |
RONEY VANDER DOS SANTOS, IQ/Unicamp; FABIAN VILLALTA-ROMERO, IQ/Unicamp, Instituto Tecnológico de Costa Rica; DANIJELA STANISIC, IQ/Unicamp; LUIZ BORRO, Unicamp, CNPTIA; GORAN NESIC, CNPTIA; LJUBICA TASIC, IQ/Unicamp. |
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Título: |
Citrus bioflavonoid, hesperetin, as inhibitor of two thrombin-like snake venom serine proteases isolated from Crotalus simus. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Toxicon, v. 143, p. 36-43, Mar. 2018. |
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DOI: |
https://doi.org/10.1016/j.toxicon.2018.01.005 |
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Idioma: |
Inglês |
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Conteúdo: |
Around 5.5 million people suffer from snakebites per year, with about 400,000 cases with some type of sequelae, such as amputation, and 20,000 to 125,000 cases with the fatal end. Usually, the victim outcome depends on correct, agile and many times in situ intervention based on the proper identification of the snake venom type and its potential effects, among other factors. Therefore, knowledge on the snake venom composition and a research on inhibitors of snake venom target components might ameliorate envenoming dangerous outcome. Herein, two thrombin-like serine proteases from the Crotalus simus snake venom - SVSP1 and SVSP2 - were isolated in two chromatographic steps, using gel filtration and then RP-HPLC. They showed molecular masses of around 31.3 and 24.6 kDa, respectively, and mostly b-sheet secondary structure features. The SVSP1 and SVSP2 were sequenced using tandem mass spectrometry (Q-TOF). Using the known serine protease structure (PDB entry: 4e7n), which was evaluated as homologous to the two target proteins, in silico docking results showed that hesperetin is its excellent inhibitor. Using in vitro tests with the commercial hesperetin, kinetic parameters were obtained for SVSPs against the synthetic substrate BApNA. Obtained results pointed that hesperetin might act as an uncompetitive (SVSP1) or mixed (SVSP2) inhibitor. Also, the fluorescence quenching upon inhibition was observed, as well as, red shift in maximums of around 20 nm, which indicate that the tryptophan residues in the target enzymes suffered conformational changes caused by hesperetin binding. Thus, a naturally occurring flavone that can easily be extracted from oranges might serve as low-cost inhibitor of the investigated snake venom proteases. MenosAround 5.5 million people suffer from snakebites per year, with about 400,000 cases with some type of sequelae, such as amputation, and 20,000 to 125,000 cases with the fatal end. Usually, the victim outcome depends on correct, agile and many times in situ intervention based on the proper identification of the snake venom type and its potential effects, among other factors. Therefore, knowledge on the snake venom composition and a research on inhibitors of snake venom target components might ameliorate envenoming dangerous outcome. Herein, two thrombin-like serine proteases from the Crotalus simus snake venom - SVSP1 and SVSP2 - were isolated in two chromatographic steps, using gel filtration and then RP-HPLC. They showed molecular masses of around 31.3 and 24.6 kDa, respectively, and mostly b-sheet secondary structure features. The SVSP1 and SVSP2 were sequenced using tandem mass spectrometry (Q-TOF). Using the known serine protease structure (PDB entry: 4e7n), which was evaluated as homologous to the two target proteins, in silico docking results showed that hesperetin is its excellent inhibitor. Using in vitro tests with the commercial hesperetin, kinetic parameters were obtained for SVSPs against the synthetic substrate BApNA. Obtained results pointed that hesperetin might act as an uncompetitive (SVSP1) or mixed (SVSP2) inhibitor. Also, the fluorescence quenching upon inhibition was observed, as well as, red shift in maximums of around 20 nm, which indicate that the try... Mostrar Tudo |
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Palavras-Chave: |
Análise in silico; Análise in vitro; Crotalus simus; Inibição enzimática; Snake venom serine proteases; Veneno de cobra. |
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Thesaurus Nal: |
Enzyme inhibition; Hesperetin. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 02656naa a2200289 a 4500
001 2093443
005 2020-01-07
008 2018 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1016/j.toxicon.2018.01.005$2DOI
100 1 $aSANTOS, R. V. dos
245 $aCitrus bioflavonoid, hesperetin, as inhibitor of two thrombin-like snake venom serine proteases isolated from Crotalus simus.$h[electronic resource]
260 $c2018
520 $aAround 5.5 million people suffer from snakebites per year, with about 400,000 cases with some type of sequelae, such as amputation, and 20,000 to 125,000 cases with the fatal end. Usually, the victim outcome depends on correct, agile and many times in situ intervention based on the proper identification of the snake venom type and its potential effects, among other factors. Therefore, knowledge on the snake venom composition and a research on inhibitors of snake venom target components might ameliorate envenoming dangerous outcome. Herein, two thrombin-like serine proteases from the Crotalus simus snake venom - SVSP1 and SVSP2 - were isolated in two chromatographic steps, using gel filtration and then RP-HPLC. They showed molecular masses of around 31.3 and 24.6 kDa, respectively, and mostly b-sheet secondary structure features. The SVSP1 and SVSP2 were sequenced using tandem mass spectrometry (Q-TOF). Using the known serine protease structure (PDB entry: 4e7n), which was evaluated as homologous to the two target proteins, in silico docking results showed that hesperetin is its excellent inhibitor. Using in vitro tests with the commercial hesperetin, kinetic parameters were obtained for SVSPs against the synthetic substrate BApNA. Obtained results pointed that hesperetin might act as an uncompetitive (SVSP1) or mixed (SVSP2) inhibitor. Also, the fluorescence quenching upon inhibition was observed, as well as, red shift in maximums of around 20 nm, which indicate that the tryptophan residues in the target enzymes suffered conformational changes caused by hesperetin binding. Thus, a naturally occurring flavone that can easily be extracted from oranges might serve as low-cost inhibitor of the investigated snake venom proteases.
650 $aEnzyme inhibition
650 $aHesperetin
653 $aAnálise in silico
653 $aAnálise in vitro
653 $aCrotalus simus
653 $aInibição enzimática
653 $aSnake venom serine proteases
653 $aVeneno de cobra
700 1 $aVILLALTA-ROMERO, F.
700 1 $aSTANISIC, D.
700 1 $aBORRO, L.
700 1 $aNESHICH, G.
700 1 $aTASIC, L.
773 $tToxicon$gv. 143, p. 36-43, Mar. 2018.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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| Registros recuperados : 8 | |
| 1. |  | SANTOS, R. V. dos; VILLALTA-ROMERO, F.; STANISIC, D.; BORRO, L.; NESHICH, G.; TASIC, L. Citrus bioflavonoid, hesperetin, as inhibitor of two thrombin-like snake venom serine proteases isolated from Crotalus simus. Toxicon, v. 143, p. 36-43, Mar. 2018.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 2. | | OLIVEIRA, R. C. DE; ROMERO, F. B.; ALVES, C. R.; BISWAS, A.; CHENG, H. N.; FURTADO, R. F. Filmes de polianilina (pani) eletropolimerizados sobre superfície de ito para uso como indicador colorimétrico para detecção da amônia; polimerização de filmes de pani como indicador da presença de amõnia. Revista da Universidade Vale do Rio Verde, Três Corações, v. 17, n. 1, 9 p. jan./jul. 2019.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 1 |
| Biblioteca(s): Embrapa Agroindústria Tropical. |
|  |
| 3. | | VILLALTA-ROMERO, F.; BORRO, l.; MANDIC, B.; ESCALANTE, T.; RUCAVADO, A.; GUTIÉRREZ, J. M.; NESHICH, G.; TASIC, L. Discovery of small molecule inhibitors for the snake venom metalloprotease BaP1 using in silico and in vitro tests. Bioorganic & Medicinal Chemistry Letters, v. 27, p. 2018-2022, 2017.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 4. | | PEREIRA, M. E. C.; LIMA, M. A. C. de; FILGUEIRAS, H. A. C.; ALVES, R. E.; AMORIM, T. B. F.; ROMERO, F. H. da C.; GONDIM, P. Identificação de pontos críticos de impacto durante operações pós-colheita num packing house de manga. Brazilian Journal of Plant Physiology, Piracicaba, v. 16, p. 10, 2004. Suplemento. Edição de 1. Workshop International de Pós-Colheita de Frutas; 2. Workshop International de Pós-Colheita de Citros, Cordeirópolis, SP, Set. 2004.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Semiárido. |
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| 5. | | AVELINO, F.; MIRANDA, I. P.; MOREIRA, T. D.; BECKER, H.; ROMERO, F. B.; TANIGUCHI, C. A. K.; MAZZETTO, S. E.; SOUZA FILHO, M. de S. M. de. The influence of the structural features of lignin-based polyurethane coatings on ammonium sulfate release: kinetics and thermodynamics of the process. Journal of Coatings Technology and Research, v. 16, n. 2, p. 449-463, 2019.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agroindústria Tropical. |
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| 6. | | SILVA, E. F. da; SILVA, G. F. da; FIGUEIREDO, E. O.; MENDONÇA, A. R. de; SILVA, J. P. M.; SANTOS, J. S.; AGUIAR, M. O.; ROMERO, F. M. B. Comportamento da restrição de distância de arraste de toras em um modelo de p-medianas aplicado ao planejamento da exploração de florestas nativas da Amazônia. In: CONGRESSO ONLINE INTERNACIONAL FLORESTAL, 1., 2021, Vitória. Anais eletrônicos... Vitória, ES : CONGRESSE.ME, 2021. p. 169-170.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Acre. |
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| 7. | | NESHICH, I. A. P.; NISHIMURA, L.; MORAES, F. R. de; SALIM, J. A.; VILLALTA-ROMERO, F.; BORRO, L.; YANO, I. H.; MAZONI, I.; TASIC, L.; JARDINE, J. G.; NESHICH, G. Computational Biology tools for identifying specific ligand binding residues for novel agrochemical and drug design. Current Protein and Peptide Science, v. 16, n. 8, p. 701-717, 2015.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 8. | | ABRAHÃO, A. A.; MACHADO, A. M. R.; FRASSONI, A.; SHEILA, B.; CARVALHO, C. H.; MIRANDA, C. A.; OLIVEIRA, D. A. de; ROMERO, F. C.; WERNECK, G.; SOUZA, G. dos S.; COUTO, H. A. R. do; ERVILHA, I. C.; VILLARDI, J. W.; DOBRE, L. G.; AMORIM, M.; NAKASHIMA, M. M.; MATTOS, P. P. de; CONNERTON, P. J.; MELO, P.; CLEMENTE, R. F.; COELHO, S. M. S. da C.; BRAZ, S. N.; CAVENDISH, T.; SILVA, T. H. da; FERREIRA, V. de P.; BARROCAS, P. R. G. Ambiente urbano. In: IBAMA. Relatório de qualidade do meio ambiente: RQMA: Brasil 2020. Brasília, DF, 2022. Cap. 7, p. 424-492. Selo ODS: ODS-1; ODS-3; ODS-4; ODS-6; ODS-8; ODS-9; ODS-11; ODS-12.| Tipo: Capítulo em Livro Técnico-Científico |
| Biblioteca(s): Embrapa Amazônia Oriental; Embrapa Florestas. |
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| Registros recuperados : 8 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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