Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition

Detalhes bibliográficos
Autor(a) principal: Ramalho, Suelem D. [UNESP]
Data de Publicação: 2019
Outros Autores: Pinto, Meri Emili F. [UNESP], Andricopulo, Renata K., Sanches, Paulo R. S. [UNESP], Silveira, Edilberto R., Cilli, Eduardo M. [UNESP], Andricopulo, Adriano D., Bolzani, Vanderlan S. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.21577/0103-5053.20190102
http://hdl.handle.net/11449/201421
Resumo: Orbitides are a class of small naturally occurring cyclic peptides with structural and functional diversities. Their chemical properties make this class feasible to be obtained by solid phase peptide synthesis (SPPS). Therefore, this synthetic accessibility enables useful application and facilitates the identification of analogues, bioactivity studies, and thus, enables them to be applied to obtain peptide libraries. The aim of this work was to investigate the effects of orbitides and their linear synthetic analogues on the migration of neonatal human foreskin fibroblasts. The screening of linear peptide analogues, originally designed from natural orbitides isolated from Jatropha species, demonstrated that some molecules (linear pohlianin B and linear ribifolin) have the potential to induce fibroblast migration and collagen deposition and may thus contribute to accelerating the processes of wound healing and tissue repair. These results also demonstrate the significance of using peptides as an important tool for the discovery of simple and novel drug scaffolds.
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spelling Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen depositionFibroblast migrationJatrophaLinear analoguesOrbitidesOrbitides are a class of small naturally occurring cyclic peptides with structural and functional diversities. Their chemical properties make this class feasible to be obtained by solid phase peptide synthesis (SPPS). Therefore, this synthetic accessibility enables useful application and facilitates the identification of analogues, bioactivity studies, and thus, enables them to be applied to obtain peptide libraries. The aim of this work was to investigate the effects of orbitides and their linear synthetic analogues on the migration of neonatal human foreskin fibroblasts. The screening of linear peptide analogues, originally designed from natural orbitides isolated from Jatropha species, demonstrated that some molecules (linear pohlianin B and linear ribifolin) have the potential to induce fibroblast migration and collagen deposition and may thus contribute to accelerating the processes of wound healing and tissue repair. These results also demonstrate the significance of using peptides as an important tool for the discovery of simple and novel drug scaffolds.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Instituto de Química Universidade Estadual Paulista (Unesp)Instituto de Física de São Carlos (IFSC) Universidade de São Paulo (USP)Departamento de Fisiologia e Farmacologia Universidade Federal do Ceará (UFC)Instituto de Química Universidade Estadual Paulista (Unesp)FAPESP: 2015/09533-7Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Universidade Federal do Ceará (UFC)Ramalho, Suelem D. [UNESP]Pinto, Meri Emili F. [UNESP]Andricopulo, Renata K.Sanches, Paulo R. S. [UNESP]Silveira, Edilberto R.Cilli, Eduardo M. [UNESP]Andricopulo, Adriano D.Bolzani, Vanderlan S. [UNESP]2020-12-12T02:32:05Z2020-12-12T02:32:05Z2019-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article2153-2161application/pdfhttp://dx.doi.org/10.21577/0103-5053.20190102Journal of the Brazilian Chemical Society, v. 30, n. 10, p. 2153-2161, 2019.1678-47900103-5053http://hdl.handle.net/11449/20142110.21577/0103-5053.20190102S0103-505320190010021532-s2.0-85076944807S0103-50532019001002153.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of the Brazilian Chemical Societyinfo:eu-repo/semantics/openAccess2024-01-07T06:22:28Zoai:repositorio.unesp.br:11449/201421Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-01-07T06:22:28Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
title Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
spellingShingle Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
Ramalho, Suelem D. [UNESP]
Fibroblast migration
Jatropha
Linear analogues
Orbitides
title_short Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
title_full Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
title_fullStr Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
title_full_unstemmed Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
title_sort Linear peptide analogues from Jatropha's orbitides promote migration of human neonatal foreskin fibroblasts in vitro and collagen deposition
author Ramalho, Suelem D. [UNESP]
author_facet Ramalho, Suelem D. [UNESP]
Pinto, Meri Emili F. [UNESP]
Andricopulo, Renata K.
Sanches, Paulo R. S. [UNESP]
Silveira, Edilberto R.
Cilli, Eduardo M. [UNESP]
Andricopulo, Adriano D.
Bolzani, Vanderlan S. [UNESP]
author_role author
author2 Pinto, Meri Emili F. [UNESP]
Andricopulo, Renata K.
Sanches, Paulo R. S. [UNESP]
Silveira, Edilberto R.
Cilli, Eduardo M. [UNESP]
Andricopulo, Adriano D.
Bolzani, Vanderlan S. [UNESP]
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade de São Paulo (USP)
Universidade Federal do Ceará (UFC)
dc.contributor.author.fl_str_mv Ramalho, Suelem D. [UNESP]
Pinto, Meri Emili F. [UNESP]
Andricopulo, Renata K.
Sanches, Paulo R. S. [UNESP]
Silveira, Edilberto R.
Cilli, Eduardo M. [UNESP]
Andricopulo, Adriano D.
Bolzani, Vanderlan S. [UNESP]
dc.subject.por.fl_str_mv Fibroblast migration
Jatropha
Linear analogues
Orbitides
topic Fibroblast migration
Jatropha
Linear analogues
Orbitides
description Orbitides are a class of small naturally occurring cyclic peptides with structural and functional diversities. Their chemical properties make this class feasible to be obtained by solid phase peptide synthesis (SPPS). Therefore, this synthetic accessibility enables useful application and facilitates the identification of analogues, bioactivity studies, and thus, enables them to be applied to obtain peptide libraries. The aim of this work was to investigate the effects of orbitides and their linear synthetic analogues on the migration of neonatal human foreskin fibroblasts. The screening of linear peptide analogues, originally designed from natural orbitides isolated from Jatropha species, demonstrated that some molecules (linear pohlianin B and linear ribifolin) have the potential to induce fibroblast migration and collagen deposition and may thus contribute to accelerating the processes of wound healing and tissue repair. These results also demonstrate the significance of using peptides as an important tool for the discovery of simple and novel drug scaffolds.
publishDate 2019
dc.date.none.fl_str_mv 2019-01-01
2020-12-12T02:32:05Z
2020-12-12T02:32:05Z
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 http://dx.doi.org/10.21577/0103-5053.20190102
Journal of the Brazilian Chemical Society, v. 30, n. 10, p. 2153-2161, 2019.
1678-4790
0103-5053
http://hdl.handle.net/11449/201421
10.21577/0103-5053.20190102
S0103-50532019001002153
2-s2.0-85076944807
S0103-50532019001002153.pdf
url http://dx.doi.org/10.21577/0103-5053.20190102
http://hdl.handle.net/11449/201421
identifier_str_mv Journal of the Brazilian Chemical Society, v. 30, n. 10, p. 2153-2161, 2019.
1678-4790
0103-5053
10.21577/0103-5053.20190102
S0103-50532019001002153
2-s2.0-85076944807
S0103-50532019001002153.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of the Brazilian Chemical Society
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 2153-2161
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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