Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis
Autor(a) principal: | |
---|---|
Data de Publicação: | 1997 |
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=S0103-50531997000100012 |
Resumo: | The classic hydrolysis procedure for quantification of resin-bound aminoacyl and peptidyl groups with 12 N HCl: propionic acid was reevaluated by studying the influence of the nature of the resin and the resin-bound group. Their stability during acid hydrolysis was dependent on the C-terminal amino acid, and the order of acid stability was Phe > Val > Gly. Otherwise, the dipeptides Ala-Gly, Ala-Val, and Ala-Phe displayed enhanced rates of hydrolysis of the resin if compared with their parent aminoacyl groups. Amongthe resins assayed, the order of acid stability was: benzhydrylamine-resin>p-methylbenzhydrylamine-resin ≅4-(oxymethyl)-phenylacetamidomethyl-resin > chloromethyl-copolymer of styrene-1%-divinylbenzene. Important for peptide synthesis method, the findings demonstrate that longer hydrolysis times than previously recommended in the literature (1 h at 130 °C and 15 min at 160 °C for peptides attached to the chloromethyl-copolymer of styrene-1%-divinylbenzene) are necessary for the quantitative acid-catalyzed cleavage of some resin-bound groups. The observed broad range of hydrolysis time varied from less than 1 h to about 100 h. |
id |
SBQ-2_e4ca6f152c3301fc038c72608d8237a6 |
---|---|
oai_identifier_str |
oai:scielo:S0103-50531997000100012 |
network_acronym_str |
SBQ-2 |
network_name_str |
Journal of the Brazilian Chemical Society (Online) |
repository_id_str |
|
spelling |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysispeptide hydrolysisresinacid hydrolysisamino acid analysisacyl-resin hydrolysissolid phase peptide synthesisThe classic hydrolysis procedure for quantification of resin-bound aminoacyl and peptidyl groups with 12 N HCl: propionic acid was reevaluated by studying the influence of the nature of the resin and the resin-bound group. Their stability during acid hydrolysis was dependent on the C-terminal amino acid, and the order of acid stability was Phe > Val > Gly. Otherwise, the dipeptides Ala-Gly, Ala-Val, and Ala-Phe displayed enhanced rates of hydrolysis of the resin if compared with their parent aminoacyl groups. Amongthe resins assayed, the order of acid stability was: benzhydrylamine-resin>p-methylbenzhydrylamine-resin ≅4-(oxymethyl)-phenylacetamidomethyl-resin > chloromethyl-copolymer of styrene-1%-divinylbenzene. Important for peptide synthesis method, the findings demonstrate that longer hydrolysis times than previously recommended in the literature (1 h at 130 °C and 15 min at 160 °C for peptides attached to the chloromethyl-copolymer of styrene-1%-divinylbenzene) are necessary for the quantitative acid-catalyzed cleavage of some resin-bound groups. The observed broad range of hydrolysis time varied from less than 1 h to about 100 h.Sociedade Brasileira de Química1997-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50531997000100012Journal of the Brazilian Chemical Society v.8 n.1 1997reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50531997000100012info:eu-repo/semantics/openAccessJubilut,Guita N.Marchetto,ReinaldoCilli,Eduardo M.Oliveira,EliandreMiranda,AntonioTominaga,MinekoNakaiee,Clóvis R.eng2011-10-04T00:00:00Zoai:scielo:S0103-50531997000100012Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2011-10-04T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
title |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
spellingShingle |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis Jubilut,Guita N. peptide hydrolysis resin acid hydrolysis amino acid analysis acyl-resin hydrolysis solid phase peptide synthesis |
title_short |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
title_full |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
title_fullStr |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
title_full_unstemmed |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
title_sort |
Comparative time-course study of aminoacyl- and dipeptidyl-resin hydrolysis |
author |
Jubilut,Guita N. |
author_facet |
Jubilut,Guita N. Marchetto,Reinaldo Cilli,Eduardo M. Oliveira,Eliandre Miranda,Antonio Tominaga,Mineko Nakaiee,Clóvis R. |
author_role |
author |
author2 |
Marchetto,Reinaldo Cilli,Eduardo M. Oliveira,Eliandre Miranda,Antonio Tominaga,Mineko Nakaiee,Clóvis R. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Jubilut,Guita N. Marchetto,Reinaldo Cilli,Eduardo M. Oliveira,Eliandre Miranda,Antonio Tominaga,Mineko Nakaiee,Clóvis R. |
dc.subject.por.fl_str_mv |
peptide hydrolysis resin acid hydrolysis amino acid analysis acyl-resin hydrolysis solid phase peptide synthesis |
topic |
peptide hydrolysis resin acid hydrolysis amino acid analysis acyl-resin hydrolysis solid phase peptide synthesis |
description |
The classic hydrolysis procedure for quantification of resin-bound aminoacyl and peptidyl groups with 12 N HCl: propionic acid was reevaluated by studying the influence of the nature of the resin and the resin-bound group. Their stability during acid hydrolysis was dependent on the C-terminal amino acid, and the order of acid stability was Phe > Val > Gly. Otherwise, the dipeptides Ala-Gly, Ala-Val, and Ala-Phe displayed enhanced rates of hydrolysis of the resin if compared with their parent aminoacyl groups. Amongthe resins assayed, the order of acid stability was: benzhydrylamine-resin>p-methylbenzhydrylamine-resin ≅4-(oxymethyl)-phenylacetamidomethyl-resin > chloromethyl-copolymer of styrene-1%-divinylbenzene. Important for peptide synthesis method, the findings demonstrate that longer hydrolysis times than previously recommended in the literature (1 h at 130 °C and 15 min at 160 °C for peptides attached to the chloromethyl-copolymer of styrene-1%-divinylbenzene) are necessary for the quantitative acid-catalyzed cleavage of some resin-bound groups. The observed broad range of hydrolysis time varied from less than 1 h to about 100 h. |
publishDate |
1997 |
dc.date.none.fl_str_mv |
1997-01-01 |
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=S0103-50531997000100012 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50531997000100012 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50531997000100012 |
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.8 n.1 1997 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_ |
1750318162981683200 |