Utilize este identificador para referenciar este registo: http://hdl.handle.net/1822/26877

TítuloDevelopment of new chimeric proteins for tissue engineering
Autor(es)Pereira, A. M.
Bernardo, T. C.
Costa, André da
Collins, Tony
Machado, Raul
Leonor, I. B.
Casal, Margarida
Reis, R. L.
Palavras-chaveChimeric protein
Recombinant DNA technology
Spider silk protein
Tissue engineering
DataSet-2013
EditoraJohn Wiley and Sons
CitaçãoPereira A. M., Bernardo T. C., Costa A., Collins T., Machado R., Leonor I. B., Casal M., Reis R. L. Development of new chimeric proteins for tissue engineering, Journal of Tissue Engineering and Regenerative Medicine, Vol. 7, Issue 1, pp. 46, doi:10.1002/term.1822, 2013
Resumo(s)Tissue engineering is an emerging !eld focused on the development of novel bioactive multifunctional materials that can be used to replace damaged and failing tissues. However, these biomaterials often present several problems such as loss of mechanical and/or biological properties and adverse immune responses. The use of natural polymers, such as proteins, provides a promising solution for these drawbacks. With advances in recombinant DNA technology and biotechnology, it is possible to design and produce new materials with different features by combining domains of different proteins in the same fusion protein. Spider dragline silk proteins have been suggested to have a large potential for many different biomedical applications due to its outstanding mechanical properties. In addition, spider silk is also biocompatible, hypoallergenic and completely biodegradable. Recently, silk copolymers based on repeats of the consensus sequence of MaSp1 (major ampullate spidroin I) from Nephila clavipes (6mer) have been fused with different functional proteins, peptides and protein motifs, showing promising results [1, 2]. In this project, by exploring the use of recombinant DNA techniques, we have constructed new silk copolymers composed of a structural motif (6mer) fused with functional domains namely GFOGER (from collagen type I) and FNII (!bronectin domain II); both are involved in cell adhesion and angiogenesis processes which are key factors in tissue engineering. Expression and puri!cation of the new chimeric proteins were successfully attained in Escherichia coli by means of auto-induction media. Furthermore, formic acid can be explored as a solvent for processing of the aforementioned recombinant copolymers. Results from the characterization of these biomaterials will be presented
TipoconferenceAbstract
DescriçãoPublicado em "Journal of Tissue Engineering and Regenerative Medicine", vol. 7, supp. 1 (2013)
URIhttp://hdl.handle.net/1822/26877
Versão da editorahttp://onlinelibrary.wiley.com/doi/10.1002/term.2013.7.issue-s1/issuetoc
Arbitragem científicayes
AcessorestrictedAccess
Aparece nas coleções:3B’s - Resumos em livros de atas de conferências - indexados no ISI Web of Science
DBio - Comunicações/Communications in Congresses

Ficheiros deste registo:
Ficheiro Descrição TamanhoFormato 
17758-AMPereira-Polaris2103.pdf42,21 kBAdobe 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