Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides

Detalhes bibliográficos
Autor(a) principal: Decandio,Carla C.
Data de Publicação: 2020
Outros Autores: Vassiliades,Sandra V., Gerbelli,Barbara B., Aguilar,Andrea M., Alves,Wendel A.
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=S0103-50532020001102200
Resumo: Hybrid-peptide hydrogel arrangements are a promising alternative to obtaining biocompatible structures at the nanoscopic scale. In this work, a new class of hybrid hydrogels was obtained through the sol-gel process based on the reaction between an amyloid-like octapeptide sequence [RF]4 (where R = arginine and F = phenylalanine) covalently bonded with glycine-linked alkoxysilanes, and hybrid silylated polyethylene glycol (PEG). 1H nuclear magnetic resonance (NMR), liquid chromatography-mass spectrometry (LC-MS), and Fourier transform infrared spectroscopy (FTIR) analyses were used, resulting in synthesized precursor/intermediate molecules. The structure of hybrid hydrogel fibers was studied by atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS), where the existence of two regions in the Guinier plot was observed, one being predominantly formed by polymer while the other one by peptide chains. The rheological measurements showed that viscoelastic parameters depend on both the amount of silane peptide in the hydrogel matrix and increased temperature. Also, the FTIR spectra indicated the coexistence of antiparallel and parallel β-sheet structure patterns into amyloid fibril hydrogels, which can be modulated by peptide-silane coupling in each formulation. The analyzed hydrogels showed thixotropic and shear-thinning rheology at physiological pH, leaving open the opportunity to topical drug delivery system applications in the future.
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spelling Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptidespeptide materialspolyethylene glycol (PEG)amyloid structuressol-gel processrheologySAXSHybrid-peptide hydrogel arrangements are a promising alternative to obtaining biocompatible structures at the nanoscopic scale. In this work, a new class of hybrid hydrogels was obtained through the sol-gel process based on the reaction between an amyloid-like octapeptide sequence [RF]4 (where R = arginine and F = phenylalanine) covalently bonded with glycine-linked alkoxysilanes, and hybrid silylated polyethylene glycol (PEG). 1H nuclear magnetic resonance (NMR), liquid chromatography-mass spectrometry (LC-MS), and Fourier transform infrared spectroscopy (FTIR) analyses were used, resulting in synthesized precursor/intermediate molecules. The structure of hybrid hydrogel fibers was studied by atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS), where the existence of two regions in the Guinier plot was observed, one being predominantly formed by polymer while the other one by peptide chains. The rheological measurements showed that viscoelastic parameters depend on both the amount of silane peptide in the hydrogel matrix and increased temperature. Also, the FTIR spectra indicated the coexistence of antiparallel and parallel β-sheet structure patterns into amyloid fibril hydrogels, which can be modulated by peptide-silane coupling in each formulation. The analyzed hydrogels showed thixotropic and shear-thinning rheology at physiological pH, leaving open the opportunity to topical drug delivery system applications in the future.Sociedade Brasileira de Química2020-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532020001102200Journal of the Brazilian Chemical Society v.31 n.11 2020reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0103-5053.20200059info:eu-repo/semantics/openAccessDecandio,Carla C.Vassiliades,Sandra V.Gerbelli,Barbara B.Aguilar,Andrea M.Alves,Wendel A.eng2020-10-27T00:00:00Zoai:scielo:S0103-50532020001102200Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2020-10-27T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
title Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
spellingShingle Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
Decandio,Carla C.
peptide materials
polyethylene glycol (PEG)
amyloid structures
sol-gel process
rheology
SAXS
title_short Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
title_full Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
title_fullStr Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
title_full_unstemmed Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
title_sort Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
author Decandio,Carla C.
author_facet Decandio,Carla C.
Vassiliades,Sandra V.
Gerbelli,Barbara B.
Aguilar,Andrea M.
Alves,Wendel A.
author_role author
author2 Vassiliades,Sandra V.
Gerbelli,Barbara B.
Aguilar,Andrea M.
Alves,Wendel A.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Decandio,Carla C.
Vassiliades,Sandra V.
Gerbelli,Barbara B.
Aguilar,Andrea M.
Alves,Wendel A.
dc.subject.por.fl_str_mv peptide materials
polyethylene glycol (PEG)
amyloid structures
sol-gel process
rheology
SAXS
topic peptide materials
polyethylene glycol (PEG)
amyloid structures
sol-gel process
rheology
SAXS
description Hybrid-peptide hydrogel arrangements are a promising alternative to obtaining biocompatible structures at the nanoscopic scale. In this work, a new class of hybrid hydrogels was obtained through the sol-gel process based on the reaction between an amyloid-like octapeptide sequence [RF]4 (where R = arginine and F = phenylalanine) covalently bonded with glycine-linked alkoxysilanes, and hybrid silylated polyethylene glycol (PEG). 1H nuclear magnetic resonance (NMR), liquid chromatography-mass spectrometry (LC-MS), and Fourier transform infrared spectroscopy (FTIR) analyses were used, resulting in synthesized precursor/intermediate molecules. The structure of hybrid hydrogel fibers was studied by atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS), where the existence of two regions in the Guinier plot was observed, one being predominantly formed by polymer while the other one by peptide chains. The rheological measurements showed that viscoelastic parameters depend on both the amount of silane peptide in the hydrogel matrix and increased temperature. Also, the FTIR spectra indicated the coexistence of antiparallel and parallel β-sheet structure patterns into amyloid fibril hydrogels, which can be modulated by peptide-silane coupling in each formulation. The analyzed hydrogels showed thixotropic and shear-thinning rheology at physiological pH, leaving open the opportunity to topical drug delivery system applications in the future.
publishDate 2020
dc.date.none.fl_str_mv 2020-11-01
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=S0103-50532020001102200
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532020001102200
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.21577/0103-5053.20200059
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.31 n.11 2020
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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