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| Registros recuperados : 23 | |
| 21. |  | ZANONI, P. R. S.; SILVEIRA, A. C. da; LIMA, E. A. de; MATTOS, P. P. de; CURTO, R. de A.; MAGALHAES, W. L. E.; LAZZAROTTO, M. Uso dos produtos da araucária: madeira e coprodutos. In: SOUSA, V. A. de; FRITZSONS, E.; PINTO JUNIOR, J. E.; AGUIAR, A. V. de (ed.). Araucária: pesquisa e desenvolvimento no Brasil. Brasília, DF: Embrapa, 2021. cap. 17, p. 337-360.| Biblioteca(s): Embrapa Florestas. |
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| 22. | | SILVEIRA, A. C da; LAZZAROTTO, M.; SIQUEIRA, G. L. de A. de; LAZZAROTTO, S. R. da S.; HORNUNG, P. S.; FERNANDES, M.; QUEIROZ, D. L. de; MIGUEL, O. G. Thermal tool for evaluation of essential oils of Eucalyptus spp susceptible and resistant to Glycaspis brimblecombei attack. In: CONGRESSO BRASILEIRO DE ANÁLISE TÉRMICA E CALORIMETRIA, 10.; CONGRESSO PAN AMERICANO DE ANÁLISE TÉRMICA E CALORIMETRIA, 4., 2016, São Paulo. Trabalhos. [S.l.]: ABRATEC, 2016. 4 p. Disponível online.| Biblioteca(s): Embrapa Florestas. |
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| 23. | | SIQUEIRA, G. L. de A. de; LAZZAROTTO, M.; FERNANDES, M.; SILVEIRA, A. C da; LAZZAROTTO, S. R. da S.; CARVALHO FILHO, M. A. da S.; LACERDA, L. G.; QUEIROZ, D. L. de; MIGUEL, O. G. Thermoanalytical evaluation of essential oils of the leaves from Eucalyptus spp susceptible and resistant to Glycaspis brimblecombei. Brazilian Journal of Thermal Analysis, v. 5, n. 1, 2016. 6 p.| Biblioteca(s): Embrapa Florestas. |
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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
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
29/01/2024 |
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Data da última atualização: |
29/01/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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Autoria: |
GUIMARÃES, C. F. R. C.; FÉLIX. A. S.; BRANDÃO, T. A. S.; BEMQUERER, M. P.; PILÓ-VELOSO, D.; VERLY, R.; RESENDE, J. M. |
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Afiliação: |
UNIVERSIDADE FEDERAL DE MINAS GERAIS; AMANDA S. FÉLIX, UNIVERSIDADE FEDERAL DOS VALES DO JEQUITINHONHA E MUCURI; TIAGO A. S. BRANDÃO, UNIVERSIDADE FEDERAL DE MINAS GERAIS; MARCELO PORTO BEMQUERER, CNPGL; DORILA PILÓ‑VELOSO, UNIVERSIDADE FEDERAL DE MINAS GERAIS; RODRIGO M. VERLY, UNIVERSIDADE FEDERAL DOS VALES DO JEQUITINHONHA E MUCURI; JARBAS M. RESENDE, UNIVERSIDADE FEDERAL DE MINAS GERAIS. |
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Título: |
Optimizing the synthesis of dimeric peptides: infuence of the reaction medium and efects that modulate kinetics and reaction yield. |
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Ano de publicação: |
2023 |
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Fonte/Imprenta: |
Amino Acids, v. 55, p. 1201-1212, 2023. |
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DOI: |
https://doi.org/10.1007/s00726-023-03309-x |
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Idioma: |
Inglês |
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Conteúdo: |
Peptides are remarkably interesting alternatives to several applications. In particular, antimicrobial sequences have raised major interest of the scientifc community due to the resistance acquired by commonly used antibiotics. Amongst these, some dimeric peptides have shown very promising characteristics as strong biological activities and resistance against degradation by peptidases. However, despite such promising characteristics, a relatively small number of studies address dimeric peptides, mainly due to the synthesis-related obstacles in their production, whereas the well-implemented routines of solid phase peptide synthesis—which includes the possibility of automation—makes life signifcantly easier. Here, we present kinetic investigations of the dimerization of a cysteine-containing sequence to obtain the homodimeric antimicrobial peptide homotarsinin. Based on the structural and membrane interaction data already available for the dimer and its monomeric chain, we have proposed distinct dimerization protocols in selected environments, namely, aqueous bufer, TFE:H2O and micellar solutions. The experimental results were adjusted by a theoretical model. Both the kinetic profles and the reaction yields are dependent on the reaction medium, clearly indicating that aggregation, peptide structure, and peptide–membrane interactions play major roles in the formation of the disulfde bond. Finally, the rationalization of the diferent aspects addressed here is expected to contribute to research and applications that demand the obtainment of dimeric peptides MenosPeptides are remarkably interesting alternatives to several applications. In particular, antimicrobial sequences have raised major interest of the scientifc community due to the resistance acquired by commonly used antibiotics. Amongst these, some dimeric peptides have shown very promising characteristics as strong biological activities and resistance against degradation by peptidases. However, despite such promising characteristics, a relatively small number of studies address dimeric peptides, mainly due to the synthesis-related obstacles in their production, whereas the well-implemented routines of solid phase peptide synthesis—which includes the possibility of automation—makes life signifcantly easier. Here, we present kinetic investigations of the dimerization of a cysteine-containing sequence to obtain the homodimeric antimicrobial peptide homotarsinin. Based on the structural and membrane interaction data already available for the dimer and its monomeric chain, we have proposed distinct dimerization protocols in selected environments, namely, aqueous bufer, TFE:H2O and micellar solutions. The experimental results were adjusted by a theoretical model. Both the kinetic profles and the reaction yields are dependent on the reaction medium, clearly indicating that aggregation, peptide structure, and peptide–membrane interactions play major roles in the formation of the disulfde bond. Finally, the rationalization of the diferent aspects addressed here is expected to contrib... Mostrar Tudo |
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Palavras-Chave: |
Aggregation; Agregação; Dimeric peptides; Disulfde bond; Estrutura peptídica; Ligação dissulfeto; Peptide structure; Peptide synthesis. |
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Thesagro: |
Energia Cinética; Peptídeo. |
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Thesaurus NAL: |
Kinetics. |
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Categoria do assunto: |
W Química e Física |
|
Marc: |
LEADER 02609naa a2200337 a 4500
001 2161434
005 2024-01-29
008 2023 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1007/s00726-023-03309-x$2DOI
100 1 $aGUIMARÃES, C. F. R. C.
245 $aOptimizing the synthesis of dimeric peptides$binfuence of the reaction medium and efects that modulate kinetics and reaction yield.$h[electronic resource]
260 $c2023
520 $aPeptides are remarkably interesting alternatives to several applications. In particular, antimicrobial sequences have raised major interest of the scientifc community due to the resistance acquired by commonly used antibiotics. Amongst these, some dimeric peptides have shown very promising characteristics as strong biological activities and resistance against degradation by peptidases. However, despite such promising characteristics, a relatively small number of studies address dimeric peptides, mainly due to the synthesis-related obstacles in their production, whereas the well-implemented routines of solid phase peptide synthesis—which includes the possibility of automation—makes life signifcantly easier. Here, we present kinetic investigations of the dimerization of a cysteine-containing sequence to obtain the homodimeric antimicrobial peptide homotarsinin. Based on the structural and membrane interaction data already available for the dimer and its monomeric chain, we have proposed distinct dimerization protocols in selected environments, namely, aqueous bufer, TFE:H2O and micellar solutions. The experimental results were adjusted by a theoretical model. Both the kinetic profles and the reaction yields are dependent on the reaction medium, clearly indicating that aggregation, peptide structure, and peptide–membrane interactions play major roles in the formation of the disulfde bond. Finally, the rationalization of the diferent aspects addressed here is expected to contribute to research and applications that demand the obtainment of dimeric peptides
650 $aKinetics
650 $aEnergia Cinética
650 $aPeptídeo
653 $aAggregation
653 $aAgregação
653 $aDimeric peptides
653 $aDisulfde bond
653 $aEstrutura peptídica
653 $aLigação dissulfeto
653 $aPeptide structure
653 $aPeptide synthesis
700 1 $aFÉLIX. A. S.
700 1 $aBRANDÃO, T. A. S.
700 1 $aBEMQUERER, M. P.
700 1 $aPILÓ-VELOSO, D.
700 1 $aVERLY, R.
700 1 $aRESENDE, J. M.
773 $tAmino Acids$gv. 55, p. 1201-1212, 2023.
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