Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/26877

TitleDevelopment of new chimeric proteins for tissue engineering
Author(s)Pereira, A. M.
Bernardo, T. C.
Costa, André da
Collins, Tony
Machado, Raul
Leonor, I. B.
Casal, Margarida
Reis, R. L.
KeywordsChimeric protein
Recombinant DNA technology
Spider silk protein
Tissue engineering
Issue dateSep-2013
PublisherJohn Wiley and Sons
CitationPereira 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
Abstract(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
TypeAbstract
DescriptionPublicado em "Journal of Tissue Engineering and Regenerative Medicine", vol. 7, supp. 1 (2013)
URIhttp://hdl.handle.net/1822/26877
Publisher versionhttp://onlinelibrary.wiley.com/doi/10.1002/term.2013.7.issue-s1/issuetoc
Peer-Reviewedyes
AccessRestricted access (UMinho)
Appears in Collections:3B’s - Resumos em livros de atas de conferências - indexados no ISI Web of Science
DBio - Comunicações/Communications in Congresses

Files in This Item:
File Description SizeFormat 
17758-AMPereira-Polaris2103.pdf
  Restricted access
42,21 kBAdobe PDFView/Open

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 ORCID