Utilize este identificador para referenciar este registo: http://hdl.handle.net/1822/38079

TítuloCo-assembly, spatiotemporal control and morphogenesis of a hybrid protein-peptide system
AutorInostroza-Brito, K. E.
Collin, E.
Siton-Mendelson, O.
Smith, K. H.
Monge-Marcet, A.
Ferreira, D. S.
Rodríguez, R. P.
Alonso, M.
Rodríguez-Cabello, J. C.
Reis, R. L.
Sagués, F.
Botto, L.
Bitton, R.
Azevedo, Helena S.
Mata, A.
Palavras-chaveBioinspired materials
Biomedical materials
Molecular self-assembly
DataSet-2015
EditoraNature
CitaçãoInostroza-Brito K. E., Collin E., Siton-Mendelson O., Smith K. H., Monge-Marcet A., Ferreira D. S., Rodríguez R. P., Alonso M., Rodríguez-Cabello J. C., Reis R. L., Sagués F., Botto L., Bitton R., Azevedo H. S., Mata A. Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein-peptide system, Nature Chemistry, Vol. 7, Issue 11, pp. 897–904, doi:doi:10.1038/nchem.2349, 2015
ResumoControlling molecular interactions between bioinspired molecules can enable the development of new materials with higher complexity and innovative properties. Here we report on a dynamic system that emerges from the conformational modification of an elastin-like protein by peptide amphiphiles and with the capacity to access, and be maintained in, non-equilibrium for substantial periods of time. The system enables the formation of a robust membrane that displays controlled assembly and disassembly capabilities, adhesion and sealing to surfaces, self-healing and the capability to undergo morphogenesis into tubular structures with high spatiotemporal control. We use advanced microscopy along with turbidity and spectroscopic measurements to investigate the mechanism of assembly and its relation to the distinctive membrane architecture and the resulting dynamic properties. Using cell-culture experiments with endothelial and adipose-derived stem cells, we demonstrate the potential of this system to generate complex bioactive scaffolds for applications such as tissue engineering.
Tipoarticle
URIhttp://hdl.handle.net/1822/38079
DOI10.1038/nchem.2349
ISSN1755-4330
1755-4349
Versão da editorahttp://www.nature.com/nchem/journal/v7/n11/full/nchem.2349.html
Arbitragem científicayes
AcessorestrictedAccess
Aparece nas coleções:3B’s - Artigos em revistas/Papers in scientific journals

Ficheiros deste registo:
Ficheiro Descrição TamanhoFormato 
18600-HAzevedo_NatureChem2015.pdf9,79 MBAdobe PDFVer/Abrir  Solicitar cópia ao autor!

Partilhe no FacebookPartilhe no TwitterPartilhe no DeliciousPartilhe no LinkedInPartilhe no DiggAdicionar ao Google BookmarksPartilhe no MySpacePartilhe no Orkut
Exporte no formato BibTex mendeley Exporte no formato Endnote Adicione ao seu Currículo DeGóis