Nanostructure formation and cell spheroid morphogenesis of a peptide supramolecular hydrogel
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , , , , |
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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oai:repositorio.unifesp.br:11600/67483 |
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Repositório Institucional da UNIFESP |
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3465 |
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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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ório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-10-05T04:01:17Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
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 |
format |
article |
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 |
bitstream.url.fl_str_mv |
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bitstream.checksumAlgorithm.fl_str_mv |
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repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1783460226127626240 |