Amino acids as selective sulfonamide acylating agents

Detalhes bibliográficos
Autor(a) principal: Gomes, P
Data de Publicação: 2003
Outros Autores: Gomes, JRB, Rodrigues, M, Moreira, R
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/10216/82048
Resumo: Acylation of antimalarial and bacteriostatic sulfonamides with N-protected amino acids and peptides was carried out using standard peptide coupling methods. These acylation reactions are regioselective for the N-4 nitrogen atom of diazine-containing sulfonamides. In contrast, only N-1 coupling was found for sulfisoxazole, an isoxazole-based sulfonamide. Computational studies suggest that a combination of geometrical, thermodynamic and electronic factors are responsible for the different reactivities reported.
id RCAP_5b9a7dcec76e5156503ab0b1eca96c76
oai_identifier_str oai:repositorio-aberto.up.pt:10216/82048
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Amino acids as selective sulfonamide acylating agentsQuímicaChemical sciencesAcylation of antimalarial and bacteriostatic sulfonamides with N-protected amino acids and peptides was carried out using standard peptide coupling methods. These acylation reactions are regioselective for the N-4 nitrogen atom of diazine-containing sulfonamides. In contrast, only N-1 coupling was found for sulfisoxazole, an isoxazole-based sulfonamide. Computational studies suggest that a combination of geometrical, thermodynamic and electronic factors are responsible for the different reactivities reported.20032003-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/82048eng0040-402010.1016/s0040-4020(03)01206-7Gomes, PGomes, JRBRodrigues, MMoreira, Rinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T13:05:23Zoai:repositorio-aberto.up.pt:10216/82048Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:33:18.926948Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Amino acids as selective sulfonamide acylating agents
title Amino acids as selective sulfonamide acylating agents
spellingShingle Amino acids as selective sulfonamide acylating agents
Gomes, P
Química
Chemical sciences
title_short Amino acids as selective sulfonamide acylating agents
title_full Amino acids as selective sulfonamide acylating agents
title_fullStr Amino acids as selective sulfonamide acylating agents
title_full_unstemmed Amino acids as selective sulfonamide acylating agents
title_sort Amino acids as selective sulfonamide acylating agents
author Gomes, P
author_facet Gomes, P
Gomes, JRB
Rodrigues, M
Moreira, R
author_role author
author2 Gomes, JRB
Rodrigues, M
Moreira, R
author2_role author
author
author
dc.contributor.author.fl_str_mv Gomes, P
Gomes, JRB
Rodrigues, M
Moreira, R
dc.subject.por.fl_str_mv Química
Chemical sciences
topic Química
Chemical sciences
description Acylation of antimalarial and bacteriostatic sulfonamides with N-protected amino acids and peptides was carried out using standard peptide coupling methods. These acylation reactions are regioselective for the N-4 nitrogen atom of diazine-containing sulfonamides. In contrast, only N-1 coupling was found for sulfisoxazole, an isoxazole-based sulfonamide. Computational studies suggest that a combination of geometrical, thermodynamic and electronic factors are responsible for the different reactivities reported.
publishDate 2003
dc.date.none.fl_str_mv 2003
2003-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/10216/82048
url https://hdl.handle.net/10216/82048
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0040-4020
10.1016/s0040-4020(03)01206-7
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
_version_ 1799135644075687936

Registros relacionados