Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD
Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate-binding modules fused to RGD
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DOI：
10.1002/jbm.a.32284
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发表时间：
2010-01-01
影响因子：
4.9
通讯作者：
Gama, F. M. P.
中科院分区：
文献类型：
--
作者：
Andrade, F. K.;Moreira, S. M. G.;Gama, F. M. P.
细胞与生物医学材料的附着可以通过使用在几种细胞外基质蛋白中发现的粘附序列，如Arg-Gly-Asp（RGD）来改善。本工作从热纤梭菌多纤维素酶体中克隆了一个含有纤维素结合模块（CBM）和细胞结合序列--RGD、GRGDY的双功能重组蛋白，并在大肠杆菌中表达。这些含有RGD的纤维素结合蛋白被纯化并用于包被细菌纤维素纤维。使用小鼠胚胎成纤维细胞培养物测试其对细胞粘附/生物相容性的影响。木葡糖酸醋杆菌（Gluconacetobacter xylinus）分泌的细菌纤维素（Bacterial Cellulose，BC）是一种性质独特、具有生物医学应用前景的物质。CBM特异性地紧密吸附在纤维素上。因此，它们是以特定和简单的方式将融合的RGD序列（或其他生物活性肽）定位到纤维素表面的有用工具。事实上，与用CBM处理的纤维素相比，成纤维细胞表现出改善的与用RGD-CBM蛋白包被的细菌纤维素片相互作用的能力，即没有粘附肽。分析了所产生的几种融合蛋白的效果。(C)2009 Wiley Periodicals，Inc. J Biomed Mater Res 92A：9-17，2010
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. (C) 2009 Wiley Periodicals, Inc. J Biomed Mater Res 92A: 9-17, 2010