Hybrid Hydrogels Based on Polyethylene Glycol Bioconjugated with Silylated-Amyloidogenic Peptides
Autor(a) principal: | |
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Data de Publicação: | 2020 |
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=S0103-50532020001102200 |
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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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 |
_version_ |
1750318183489732608 |