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 | Acesso ao texto completo restrito à biblioteca da Embrapa Florestas. Para informações adicionais entre em contato com cnpf.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
10/01/2022 |
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Data da última atualização: |
14/02/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
LOURENÇON, T. V.; LIMA, G. G. de; RIBEIRO, C. S. P.; HANSEL, F. A.; MACIEL, G. M.; SILVA, K. da; WINNISCHOFER, S. M. B.; BOLZON DE MUNIZ, G. I.; MAGALHAES, W. L. E. |
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Afiliação: |
TAINISE V. LOURENÇON, Doutoranda da UFPR; GABRIEL G. DE LIMA, Pós-doutorando da UFPR; CAROLINA S. P. RIBEIRO, UFPR; FABRICIO AUGUSTO HANSEL, CNPF; GISELLE M. MACIEL, UFPR; KRISLE DA SILVA, CNPF; SHEILA M. B. WINNISCHOFER, UTFPR; GRACIELA I. BOLZON DE MUNIZ, UFPR; WASHINGTON LUIZ ESTEVES MAGALHAES, CNPF. |
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Título: |
Antioxidant, antibacterial and antitumoural activities of kraft lignin fromhardwood fractionated by acid precipitation. |
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Ano de publicação: |
2021 |
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Fonte/Imprenta: |
International Journal of Biological Macromolecules, v. 166, p. 1535-1542, Jan. 2021. |
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DOI: |
https://doi.org/10.1016/j.ijbiomac.2020.11.033 |
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Idioma: |
Inglês |
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Conteúdo: |
Kraft lignin, so far useful for energy generation, has been gathering considerable attention as an alternative ma-terial to replace fossil-based resources mainly due to its high phenolic content. However, the wide molecularweight distribution and chemical composition heterogeneity led to the development of fractionation methods.Herein, to narrow such characteristics weusedeucalypt kraft lignin fractionated atpH's 9,7, 5 and 3 bysequentialacid precipitation. These lignin fractions werefirst characterised by simultaneous pyrolysis andtrimethylsilylation (SPyT) with N-Methyl-N-(trimethylsilyl) trifluoroacetamide with posterior tests of antioxi-dant, antibacterial, and antitumour activities. We observed higher ratio of syringyl/guaiacyl groups and increasein antioxidant activity in those fractions with lower molecular weight (precipitated at lower pH's). Fractions pre-cipitated at pH's 9 and 7 have shown an outstanding antibacterial activity againstfive bacteria. Moreover, frac-tions 7 and 5 presented at cytotoxicity tests higher ability to inhibit the growth of U87MG and T98G gliomacells, while only a slight inhibition of adult humanfibroblasts (non-tumour cells) was detected. |
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Palavras-Chave: |
Antibacterial; Antitumoral; Antitumoural; Hardwood lignin; IC50; Radical scavenging; Technical lignin. |
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Thesagro: |
Antioxidante; Bactericida; Lignina. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 02271naa a2200349 a 4500
001 2138967
005 2022-02-14
008 2021 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1016/j.ijbiomac.2020.11.033$2DOI
100 1 $aLOURENÇON, T. V.
245 $aAntioxidant, antibacterial and antitumoural activities of kraft lignin fromhardwood fractionated by acid precipitation.$h[electronic resource]
260 $c2021
520 $aKraft lignin, so far useful for energy generation, has been gathering considerable attention as an alternative ma-terial to replace fossil-based resources mainly due to its high phenolic content. However, the wide molecularweight distribution and chemical composition heterogeneity led to the development of fractionation methods.Herein, to narrow such characteristics weusedeucalypt kraft lignin fractionated atpH's 9,7, 5 and 3 bysequentialacid precipitation. These lignin fractions werefirst characterised by simultaneous pyrolysis andtrimethylsilylation (SPyT) with N-Methyl-N-(trimethylsilyl) trifluoroacetamide with posterior tests of antioxi-dant, antibacterial, and antitumour activities. We observed higher ratio of syringyl/guaiacyl groups and increasein antioxidant activity in those fractions with lower molecular weight (precipitated at lower pH's). Fractions pre-cipitated at pH's 9 and 7 have shown an outstanding antibacterial activity againstfive bacteria. Moreover, frac-tions 7 and 5 presented at cytotoxicity tests higher ability to inhibit the growth of U87MG and T98G gliomacells, while only a slight inhibition of adult humanfibroblasts (non-tumour cells) was detected.
650 $aAntioxidante
650 $aBactericida
650 $aLignina
653 $aAntibacterial
653 $aAntitumoral
653 $aAntitumoural
653 $aHardwood lignin
653 $aIC50
653 $aRadical scavenging
653 $aTechnical lignin
700 1 $aLIMA, G. G. de
700 1 $aRIBEIRO, C. S. P.
700 1 $aHANSEL, F. A.
700 1 $aMACIEL, G. M.
700 1 $aSILVA, K. da
700 1 $aWINNISCHOFER, S. M. B.
700 1 $aBOLZON DE MUNIZ, G. I.
700 1 $aMAGALHAES, W. L. E.
773 $tInternational Journal of Biological Macromolecules$gv. 166, p. 1535-1542, Jan. 2021.
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Registro original: |
Embrapa Florestas (CNPF) |
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| Acesso ao texto completo restrito à biblioteca da Embrapa Gado de Leite. Para informações adicionais entre em contato com cnpgl.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
01/12/2022 |
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Data da última atualização: |
01/12/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
SOUSA, N. A. de; MARANI, M. M.; LOPES, A. L. F.; SILVA, E. M.; BARBOSA, E. A.; VASCONCELOS, A. G.; KUZNIEWSKI, F. T. B.; LUSTOSA, S. S.; GOMES, K. P.; COLUGNATI, D. B.; ROCHA, J. A.; SANTOS, L. H.; BEMQUERER, M. P.; QUELEMES, P.; VÉRAS, L.; MOREIRA, D. C.; GADELHA, K. K. L.; MAGALHÃES, P. J. C.; PLÁCIDO, A.; EATON, E.; NICOLAU, L.; MEDEIROS, J. V. R.; LEITE, J. R. S. A. |
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Afiliação: |
NAYARA ALVES DE SOUSA, Universidade Federal do Delta do Parnaíba; MARIELA M. MARANI, IPEEC-CONICET; ANDRÉ LUÍS FERNANDES LOPES, Universidade Federal do Delta do Parnaíba; EMANUELLE MORAIS SILVA, Universidade Federal do Delta do Parnaíba; EDER ALVES BARBOSA, Universidade de Brasília; ANDREANNE GOMES VASCONCELOS, Universidade de Brasília; FELIPE T. B. KUZNIEWSKI, Universidade de Brasília; SUELLEN SOUSA LUSTOSA, Universidade Federal do Delta do Parnaíba; KARINA PEREIRA GOMES, Universidade Federal de Goiás; DIEGO BASILE COLUGNATI, Universidade Federal de Goiás; JEFFERSON A. ROCHA, Universidade Federal do Maranhão; LUCIANNA HELENE SANTOS, Universidade Federal de Minas Gerais; MARCELO PORTO BEMQUERER, CNPGL; PATRICK QUELEMES, Universidade Federal do Delta do Parnaíba; LEIZ VÉRAS, Universidade Federal do Delta do Parnaíba; DANIEL C. MOREIRA, Universidade de Brasília; KALINNE KELLY LIMA GADELHA, Universidade Federal do Ceará; PEDRO JORGE CALDAS MAGALHÃES, Universidade Federal do Ceará; ALEXANDRA PLÁCIDO, Universidade do Porto; PETER EATON, Universidade do Porto; LUCAS NICOLAU, Universidade Federal do Delta do Parnaíba; JAND VENES R. MEDEIROS, Universidade Federal do Delta do Parnaíba; JOSÉ R. S. A. LEITE, Universidade de Brasília. |
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Título: |
BR-bombesin: a novel bombesin-related peptide from the skin secretion of the Chaco tree frog (Boana raniceps) with physiological gastric effects. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Amino Acids, v. 54, p. 733-747, 2022. |
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DOI: |
https://doi.org/10.1007/s00726-021-03114-4 |
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Idioma: |
Inglês |
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Conteúdo: |
Bombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bombesin in disorders that involve gastrointestinal tract motility and acid gastric secretion. MenosBombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bo... Mostrar Tudo |
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Palavras-Chave: |
Peptídeo bioativo; Secreção gástrica. |
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Thesagro: |
Anfíbio; Peptídeo. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02899naa a2200445 a 4500
001 2149045
005 2022-12-01
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1007/s00726-021-03114-4$2DOI
100 1 $aSOUSA, N. A. de
245 $aBR-bombesin$ba novel bombesin-related peptide from the skin secretion of the Chaco tree frog (Boana raniceps) with physiological gastric effects.$h[electronic resource]
260 $c2022
520 $aBombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bombesin in disorders that involve gastrointestinal tract motility and acid gastric secretion.
650 $aAnfíbio
650 $aPeptídeo
653 $aPeptídeo bioativo
653 $aSecreção gástrica
700 1 $aMARANI, M. M.
700 1 $aLOPES, A. L. F.
700 1 $aSILVA, E. M.
700 1 $aBARBOSA, E. A.
700 1 $aVASCONCELOS, A. G.
700 1 $aKUZNIEWSKI, F. T. B.
700 1 $aLUSTOSA, S. S.
700 1 $aGOMES, K. P.
700 1 $aCOLUGNATI, D. B.
700 1 $aROCHA, J. A.
700 1 $aSANTOS, L. H.
700 1 $aBEMQUERER, M. P.
700 1 $aQUELEMES, P.
700 1 $aVÉRAS, L.
700 1 $aMOREIRA, D. C.
700 1 $aGADELHA, K. K. L.
700 1 $aMAGALHÃES, P. J. C.
700 1 $aPLÁCIDO, A.
700 1 $aEATON, E.
700 1 $aNICOLAU, L.
700 1 $aMEDEIROS, J. V. R.
700 1 $aLEITE, J. R. S. A.
773 $tAmino Acids$gv. 54, p. 733-747, 2022.
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