Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel

Detalhes bibliográficos
Autor(a) principal: da Silva, Emerson [UNIFESP]
Data de Publicação: 2022
Outros Autores: Mello, Lucas R. [UNIFESP], Carrascosa, Vinicius [UNIFESP], Oliveira, Eduardo R. L. [UNIFESP], Juliano, Maria A. [UNIFESP], Hamley, Ian W., Castelletto, Valeria, Vassiliades, Sandra V., Alves, Wendel A., Nakaie, Clovis R. [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: https://pubs.acs.org/doi/10.1021/acs.langmuir.1c03215
https://repositorio.unifesp.br/11600/67483
https://doi.org/10.1021/acs.langmuir.1c03215
Resumo: Peptide-based hydrogels have attracted much attention due to their extraordinary applications in biomedicine and offer an excellent mimic for the 3D microenvironment of the extracellular matrix. These hydrated matrices comprise fibrous networks held together by a delicate balance of intermolecular forces. Here, we investigate the hydrogelation behavior of a designed decapeptide containing a tetra-leucine self-assembling backbone and fibronectin-related tripeptides near to both ends of the strand. We have observed that this synthetic peptide can to produce hydrogel matrices entrapping > 99% wt/vol% water. Ultrastructural analysis combining atomic force microscopy (AFM), small-angle neutron scattering (SANS) and X-ray diffraction revealed that amyloid-like fibrils form crosslinked networks endowed with remarkable thermal stability, the structure of which structure is not disrupted up to temperatures > 80 °C. We also examined the interaction of peptide hydrogels with either NIH3T3 mouse fibroblasts or HeLa cells and discovered that the matrices sustain cell viability and induce morphogenesis into grape-like cell spheroids. The results presented here show that this decapeptide is a remarkable building block to prepare highly stable scaffolds simultaneously endowed with high water retention capacity and the ability to instruct cell growth into tumor-like spheroids even in non-carcinoma lineages.
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spelling da Silva, Emerson [UNIFESP]Mello, Lucas R. [UNIFESP]Carrascosa, Vinicius [UNIFESP]Oliveira, Eduardo R. L. [UNIFESP]Juliano, Maria A. [UNIFESP]Hamley, Ian W.Castelletto, ValeriaVassiliades, Sandra V.Alves, Wendel A.Nakaie, Clovis R. [UNIFESP]http://lattes.cnpq.br/78005892064573262023-05-11T12:23:14Z2023-05-11T12:23:14Z2022-03-11https://pubs.acs.org/doi/10.1021/acs.langmuir.1c03215https://repositorio.unifesp.br/11600/67483https://doi.org/10.1021/acs.langmuir.1c03215Peptide-based hydrogels have attracted much attention due to their extraordinary applications in biomedicine and offer an excellent mimic for the 3D microenvironment of the extracellular matrix. These hydrated matrices comprise fibrous networks held together by a delicate balance of intermolecular forces. Here, we investigate the hydrogelation behavior of a designed decapeptide containing a tetra-leucine self-assembling backbone and fibronectin-related tripeptides near to both ends of the strand. We have observed that this synthetic peptide can to produce hydrogel matrices entrapping > 99% wt/vol% water. Ultrastructural analysis combining atomic force microscopy (AFM), small-angle neutron scattering (SANS) and X-ray diffraction revealed that amyloid-like fibrils form crosslinked networks endowed with remarkable thermal stability, the structure of which structure is not disrupted up to temperatures > 80 °C. We also examined the interaction of peptide hydrogels with either NIH3T3 mouse fibroblasts or HeLa cells and discovered that the matrices sustain cell viability and induce morphogenesis into grape-like cell spheroids. The results presented here show that this decapeptide is a remarkable building block to prepare highly stable scaffolds simultaneously endowed with high water retention capacity and the ability to instruct cell growth into tumor-like spheroids even in non-carcinoma lineages.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)19/20907-73434-3445engAmerican Chemical SocietyLangmuirHydrogelPeptideExtra-cellular matrixNanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogelinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article3811info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPEscola Paulista de Medicina (EPM)Ciências Biológicas (Biologia Molecular)BiofísicaBiofísica 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dc.title.en.fl_str_mv Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
title Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
spellingShingle Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
da Silva, Emerson [UNIFESP]
Hydrogel
Peptide
Extra-cellular matrix
title_short Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
title_full Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
title_fullStr Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
title_full_unstemmed Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
title_sort Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
author da Silva, Emerson [UNIFESP]
author_facet da Silva, Emerson [UNIFESP]
Mello, Lucas R. [UNIFESP]
Carrascosa, Vinicius [UNIFESP]
Oliveira, Eduardo R. L. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Hamley, Ian W.
Castelletto, Valeria
Vassiliades, Sandra V.
Alves, Wendel A.
Nakaie, Clovis R. [UNIFESP]
author_role author
author2 Mello, Lucas R. [UNIFESP]
Carrascosa, Vinicius [UNIFESP]
Oliveira, Eduardo R. L. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Hamley, Ian W.
Castelletto, Valeria
Vassiliades, Sandra V.
Alves, Wendel A.
Nakaie, Clovis R. [UNIFESP]
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.authorLattes.pt_BR.fl_str_mv http://lattes.cnpq.br/7800589206457326
dc.contributor.author.fl_str_mv da Silva, Emerson [UNIFESP]
Mello, Lucas R. [UNIFESP]
Carrascosa, Vinicius [UNIFESP]
Oliveira, Eduardo R. L. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Hamley, Ian W.
Castelletto, Valeria
Vassiliades, Sandra V.
Alves, Wendel A.
Nakaie, Clovis R. [UNIFESP]
dc.subject.eng.fl_str_mv Hydrogel
Peptide
Extra-cellular matrix
topic Hydrogel
Peptide
Extra-cellular matrix
description Peptide-based hydrogels have attracted much attention due to their extraordinary applications in biomedicine and offer an excellent mimic for the 3D microenvironment of the extracellular matrix. These hydrated matrices comprise fibrous networks held together by a delicate balance of intermolecular forces. Here, we investigate the hydrogelation behavior of a designed decapeptide containing a tetra-leucine self-assembling backbone and fibronectin-related tripeptides near to both ends of the strand. We have observed that this synthetic peptide can to produce hydrogel matrices entrapping > 99% wt/vol% water. Ultrastructural analysis combining atomic force microscopy (AFM), small-angle neutron scattering (SANS) and X-ray diffraction revealed that amyloid-like fibrils form crosslinked networks endowed with remarkable thermal stability, the structure of which structure is not disrupted up to temperatures > 80 °C. We also examined the interaction of peptide hydrogels with either NIH3T3 mouse fibroblasts or HeLa cells and discovered that the matrices sustain cell viability and induce morphogenesis into grape-like cell spheroids. The results presented here show that this decapeptide is a remarkable building block to prepare highly stable scaffolds simultaneously endowed with high water retention capacity and the ability to instruct cell growth into tumor-like spheroids even in non-carcinoma lineages.
publishDate 2022
dc.date.issued.fl_str_mv 2022-03-11
dc.date.accessioned.fl_str_mv 2023-05-11T12:23:14Z
dc.date.available.fl_str_mv 2023-05-11T12:23:14Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.pt_BR.fl_str_mv https://pubs.acs.org/doi/10.1021/acs.langmuir.1c03215
dc.identifier.uri.fl_str_mv https://repositorio.unifesp.br/11600/67483
dc.identifier.doi.pt_BR.fl_str_mv https://doi.org/10.1021/acs.langmuir.1c03215
url https://pubs.acs.org/doi/10.1021/acs.langmuir.1c03215
https://repositorio.unifesp.br/11600/67483
https://doi.org/10.1021/acs.langmuir.1c03215
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartof.none.fl_str_mv Langmuir
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 3434-3445
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
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