Yang Mingying, Yamauchi Kazuo, Kurokawa Masato, Asakura Tetsuo
Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo, Japan.
Tissue Eng. 2007 Dec;13(12):2941-7. doi: 10.1089/ten.2006.0448.
To develop biomaterials for tissue engineering, a silk-like protein inspired by mussel-adhesive proteins (MAPs) was designed and prepared. The primary structure of this silk-like protein is designed as TSAKPSYPPTYKAS (GAGAGS)(3) by combining the sequences (GAGAGS)(3), the crystalline region of Bombyx mori silk fibroin, and AKPSYPPTYK, the adhesive sequence of MAP from Mytilus edulis. This protein was synthesized by the genetic engineering method. Solid-state (13)C NMR spectra showed that this silk-like protein adopts flexible conformation due to introduction of the sequence AKPSYPPTYK. Cell assay indicated that this silk-like protein has significantly higher cell adhesion activities in response to normal human dermal fibroblasts (NHDFs) than Pronectin F, which is available as commercialized cell-adhesive silk-like protein. Thus, combination of remarkably high cell-adhesive activity from MAP with superiority of silk fibroin provides potentiality for application to the field of biomaterials.
为了开发用于组织工程的生物材料，设计并制备了一种受贻贝粘附蛋白（MAPs）启发的类丝蛋白。这种类丝蛋白的一级结构被设计为TSAKPSYPPTYKAS (GAGAGS)(3)，它是通过将家蚕丝丝素蛋白的结晶区域序列(GAGAGS)(3)与可食贻贝的MAP粘附序列AKPSYPPTYK相结合而得到的。该蛋白通过基因工程方法合成。固态(13)C NMR光谱表明，由于引入了序列AKPSYPPTYK，这种类丝蛋白呈现出柔性构象。细胞实验表明，与作为商业化细胞粘附类丝蛋白的Pronectin F相比，这种类丝蛋白对正常人皮肤成纤维细胞（NHDFs）具有显著更高的细胞粘附活性。因此，MAP的显著高细胞粘附活性与丝素蛋白的优势相结合，为生物材料领域的应用提供了潜力。
