Use of the same polymer for synthesis and purification of peptides
Autor(a) principal: | |
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Data de Publicação: | 2005 |
Outros Autores: | , , , , |
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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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 |
_version_ |
1750318166151528448 |