Use of the same polymer for synthesis and purification of peptides

Detalhes bibliográficos
Autor(a) principal: Silva,Elias H.
Data de Publicação: 2005
Outros Autores: Etchegaray,Augusto, Carvalho,Regina S. H., Jubilut,Guita N., Miranda,Antonio, Nakaie,Clovis R.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Journal of the Brazilian Chemical Society (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532005000200008
Resumo: This work reveals an uncommon but valuable biotechnological approach regarding the use of a same polymer (benzhydrylamine-resin, BHAR) for synthesis and anion exchange purification of peptides. Initially, the octapeptide DRVYIHPF-NH2 was synthesized in 1% and 3% cross-linked BHAR, attaching 2.5 mmol g-1 ammonium groups. Due certainly to its less rigid polymeric backbone, higher synthesis yield (about 80%) was achieved with the former resin. Next, the negatively charged peptides DEVYEHPF-NH2 and DEVYEDPF-NH2 (-1 and -3 in neutral pH, respectively), both synthesized in 1% BHAR were submitted to chromatographic separation test in this same type of resin (1% and 3%). Following comparative results of peptide synthesis and swelling data of resin beads obtained by microscopy, an improved separation of both peptides occurred with 1% BHAR batch. These findings demonstrated that BHAR applied so far for peptide synthesis, when containing high amount of positively charged ammonium groups, can be also used alternatively as a solid support for chromatographic purification of this type of biological molecule.
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spelling Use of the same polymer for synthesis and purification of peptidespeptide synthesisresinanion exchange chromatographypolymersolvent polarityThis work reveals an uncommon but valuable biotechnological approach regarding the use of a same polymer (benzhydrylamine-resin, BHAR) for synthesis and anion exchange purification of peptides. Initially, the octapeptide DRVYIHPF-NH2 was synthesized in 1% and 3% cross-linked BHAR, attaching 2.5 mmol g-1 ammonium groups. Due certainly to its less rigid polymeric backbone, higher synthesis yield (about 80%) was achieved with the former resin. Next, the negatively charged peptides DEVYEHPF-NH2 and DEVYEDPF-NH2 (-1 and -3 in neutral pH, respectively), both synthesized in 1% BHAR were submitted to chromatographic separation test in this same type of resin (1% and 3%). Following comparative results of peptide synthesis and swelling data of resin beads obtained by microscopy, an improved separation of both peptides occurred with 1% BHAR batch. These findings demonstrated that BHAR applied so far for peptide synthesis, when containing high amount of positively charged ammonium groups, can be also used alternatively as a solid support for chromatographic purification of this type of biological molecule.Sociedade Brasileira de Química2005-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532005000200008Journal of the Brazilian Chemical Society v.16 n.2 2005reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532005000200008info:eu-repo/semantics/openAccessSilva,Elias H.Etchegaray,AugustoCarvalho,Regina S. H.Jubilut,Guita N.Miranda,AntonioNakaie,Clovis R.eng2005-05-24T00:00:00Zoai:scielo:S0103-50532005000200008Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2005-05-24T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Use of the same polymer for synthesis and purification of peptides
title Use of the same polymer for synthesis and purification of peptides
spellingShingle Use of the same polymer for synthesis and purification of peptides
Silva,Elias H.
peptide synthesis
resin
anion exchange chromatography
polymer
solvent polarity
title_short Use of the same polymer for synthesis and purification of peptides
title_full Use of the same polymer for synthesis and purification of peptides
title_fullStr Use of the same polymer for synthesis and purification of peptides
title_full_unstemmed Use of the same polymer for synthesis and purification of peptides
title_sort Use of the same polymer for synthesis and purification of peptides
author Silva,Elias H.
author_facet Silva,Elias H.
Etchegaray,Augusto
Carvalho,Regina S. H.
Jubilut,Guita N.
Miranda,Antonio
Nakaie,Clovis R.
author_role author
author2 Etchegaray,Augusto
Carvalho,Regina S. H.
Jubilut,Guita N.
Miranda,Antonio
Nakaie,Clovis R.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Silva,Elias H.
Etchegaray,Augusto
Carvalho,Regina S. H.
Jubilut,Guita N.
Miranda,Antonio
Nakaie,Clovis R.
dc.subject.por.fl_str_mv peptide synthesis
resin
anion exchange chromatography
polymer
solvent polarity
topic peptide synthesis
resin
anion exchange chromatography
polymer
solvent polarity
description This work reveals an uncommon but valuable biotechnological approach regarding the use of a same polymer (benzhydrylamine-resin, BHAR) for synthesis and anion exchange purification of peptides. Initially, the octapeptide DRVYIHPF-NH2 was synthesized in 1% and 3% cross-linked BHAR, attaching 2.5 mmol g-1 ammonium groups. Due certainly to its less rigid polymeric backbone, higher synthesis yield (about 80%) was achieved with the former resin. Next, the negatively charged peptides DEVYEHPF-NH2 and DEVYEDPF-NH2 (-1 and -3 in neutral pH, respectively), both synthesized in 1% BHAR were submitted to chromatographic separation test in this same type of resin (1% and 3%). Following comparative results of peptide synthesis and swelling data of resin beads obtained by microscopy, an improved separation of both peptides occurred with 1% BHAR batch. These findings demonstrated that BHAR applied so far for peptide synthesis, when containing high amount of positively charged ammonium groups, can be also used alternatively as a solid support for chromatographic purification of this type of biological molecule.
publishDate 2005
dc.date.none.fl_str_mv 2005-04-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532005000200008
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532005000200008
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0103-50532005000200008
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Journal of the Brazilian Chemical Society v.16 n.2 2005
reponame:Journal of the Brazilian Chemical Society (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Journal of the Brazilian Chemical Society (Online)
collection Journal of the Brazilian Chemical Society (Online)
repository.name.fl_str_mv Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv ||office@jbcs.sbq.org.br
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