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Registro Completo |
Biblioteca(s): |
Embrapa Gado de Leite. |
Data corrente: |
29/01/2024 |
Data da última atualização: |
29/01/2024 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
GUIMARÃES, C. F. R. C.; FÉLIX. A. S.; BRANDÃO, T. A. S.; BEMQUERER, M. P.; PILÓ-VELOSO, D.; VERLY, R.; RESENDE, J. M. |
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. |
Título: |
Optimizing the synthesis of dimeric peptides: infuence of the reaction medium and efects that modulate kinetics and reaction yield. |
Ano de publicação: |
2023 |
Fonte/Imprenta: |
Amino Acids, v. 55, p. 1201-1212, 2023. |
DOI: |
https://doi.org/10.1007/s00726-023-03309-x |
Idioma: |
Inglês |
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 |
Palavras-Chave: |
Aggregation; Agregação; Dimeric peptides; Disulfde bond; Estrutura peptídica; Ligação dissulfeto; Peptide structure; Peptide synthesis. |
Thesagro: |
Energia Cinética; Peptídeo. |
Thesaurus Nal: |
Kinetics. |
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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| 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. |
Data corrente: |
05/02/2014 |
Data da última atualização: |
05/02/2024 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
TEIXEIRA, J. A.; RIBEIRO, J. B.; GONÇALVES, D. B.; QUEIROZ, M. V. de; ARAÚJO, E. F. de. |
Afiliação: |
JANAINA APARECIDA TEIXEIRA, UFV; JOAO BATISTA RIBEIRO, CNPGL; DANIEL BONOTO GONÇALVES, UFSJ; MARISA VIEIRA DE QUEIROZ, UFV; ELZA FERNANDES DE ARAÚJO, UFV. |
Título: |
Overproduction of polygalacturonase by Penicillium griseoroseum recombinant strains and functional analysis by targeted disruption of the pgg2 gene. |
Ano de publicação: |
2013 |
Fonte/Imprenta: |
Applied Biochemistry and Biotechnology, v. 169, n. 6, p. 1965-1977, 2013. |
DOI: |
https://doi.org/10.1007/s12010-013-0121-6 |
Idioma: |
Inglês |
Conteúdo: |
Inactivation of the pgg2 gene, a polygalacturonase-encoding gene from Penicillium griseoroseum, reduced the total activity of polygalacturonase (PG) by 90 % in wild-type P. griseoroseum, which indicates that the pgg2 gene is the major gene responsible for PG production in this species. To increase PG production, the coding region of the pgg2 gene was cloned under the control of the glyceraldehyde 3-phosphate dehydrogenase (gpd) promoter and the terminator region of the tryptophan synthase (trpC) gene from Aspergillus nidulans (pAN52pgg2 vector). This vector was then used to transform P. griseoroseum. The transformed strains were characterized according to PG production using glucose, sucrose, or sugar cane juice as the carbon sources. The recombinant P. griseoroseum T146 strain contained an additional copy of the pgg2 gene, which resulted in a 12-fold increase in PG activity when compared with that detected in the supernatant of the control PG63 strain. The proteins secreted by the recombinant strain T146 showed a strong band at 38 kDa, which corresponds to the molecular weight of PG of the P. griseoroseum. The results demonstrate the significant biotechnological potential of recombinant P. griseoroseum T146 for use in PG production. |
Palavras-Chave: |
Gene inactivation; Gpd promoter; Overproduction; Penicillium griseoroseum. |
Thesaurus NAL: |
polygalacturonase. |
Categoria do assunto: |
W Química e Física |
Marc: |
LEADER 02088naa a2200241 a 4500 001 1978792 005 2024-02-05 008 2013 bl uuuu u00u1 u #d 024 7 $ahttps://doi.org/10.1007/s12010-013-0121-6$2DOI 100 1 $aTEIXEIRA, J. A. 245 $aOverproduction of polygalacturonase by Penicillium griseoroseum recombinant strains and functional analysis by targeted disruption of the pgg2 gene.$h[electronic resource] 260 $c2013 520 $aInactivation of the pgg2 gene, a polygalacturonase-encoding gene from Penicillium griseoroseum, reduced the total activity of polygalacturonase (PG) by 90 % in wild-type P. griseoroseum, which indicates that the pgg2 gene is the major gene responsible for PG production in this species. To increase PG production, the coding region of the pgg2 gene was cloned under the control of the glyceraldehyde 3-phosphate dehydrogenase (gpd) promoter and the terminator region of the tryptophan synthase (trpC) gene from Aspergillus nidulans (pAN52pgg2 vector). This vector was then used to transform P. griseoroseum. The transformed strains were characterized according to PG production using glucose, sucrose, or sugar cane juice as the carbon sources. The recombinant P. griseoroseum T146 strain contained an additional copy of the pgg2 gene, which resulted in a 12-fold increase in PG activity when compared with that detected in the supernatant of the control PG63 strain. The proteins secreted by the recombinant strain T146 showed a strong band at 38 kDa, which corresponds to the molecular weight of PG of the P. griseoroseum. The results demonstrate the significant biotechnological potential of recombinant P. griseoroseum T146 for use in PG production. 650 $apolygalacturonase 653 $aGene inactivation 653 $aGpd promoter 653 $aOverproduction 653 $aPenicillium griseoroseum 700 1 $aRIBEIRO, J. B. 700 1 $aGONÇALVES, D. B. 700 1 $aQUEIROZ, M. V. de 700 1 $aARAÚJO, E. F. de 773 $tApplied Biochemistry and Biotechnology$gv. 169, n. 6, p. 1965-1977, 2013.
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