Improving the affinity of fibroblasts for bacterial cellulose using carbohydrat...

• Author(s): Andrade, Fábia K. ; Moreira, Susana ; Domingues, Lucília ; Gama, F. M.
• Date: 2010
• Persistent ID: http://hdl.handle.net/1822/10230
• Origin: RepositóriUM - Universidade do Minho
• Subject(s): Bacterial cellulose; CBM; Fibroblasts; RGD; Cell adhesion
• Document Type: Article
• Language: English

Description

The attachment of cells to biomedical materials can be improved by using adhesion sequences, such as Arg-Gly-Asp (RGD), found in several extracellular matrix proteins. In this work, bifunctional recombinant proteins, with a Cellulose-Binding Module (CBM), from the cellulosome of Clostridium thermocellum and cell binding sequences - RGD, GRGDY - were cloned and expressed in E.coli. These RGD-containing cellulose binding proteins were purified and used to coat bacterial cellulose fibres. Its effect on the cell adhesion/biocompatibility properties was tested using a mouse embryo fibroblasts culture. Bacterial cellulose (BC) secreted by Gluconacetobacter xylinus (=Acetobacter xylinum) is a material with unique properties and promising biomedical applications. CBMs adsorbs specifically and tightly on cellulose. Thus, they are a useful tool to address the fused RGD sequence (or other bioactive peptides) to the cellulose surface, in a specific and simple way. Indeed, fibroblasts exhibit improved ability to interact with bacterial cellulose sheets coated with RGD-CBM proteins, as compared with cellulose treated with the CBM, that is, without the adhesion peptide. The effect of the several fusion proteins produced was analyzed.