中文摘要：

人血管内皮生长因子VEGF183（132—158）肽段含有细胞外基质结合序列与纤溶酶、基质金属蛋白酶以及UPA酶裂解位点，研究该肽段作为一种蛋白药物的缓释载体，在体内既可和细胞外基质结合，又可在体内的相应酶作用下，缓慢释放。该研究以绿色荧光蛋白GFP为指示分子，进一步采用加端PCR方法将VEGF183（132—158）肽段连到GFP的C端，原核表达并纯化该融合蛋白，通过与琼脂糖肝素柱结合实验与冷冻切片的荧光显微镜观察，发现该肽段赋予了GFP蛋白结合琼脂糖肝素柱与细胞外基质的功能，GFP融合蛋白的获得为下一步的体内释放研究打下了基础。

英文摘要：

The peptide from VEGF183（132-158） containing the sequence that can bind with the extracelluar matrix, plasmin, MMP and uPA enzyme cleavage sites, can be used as one kind of protein drug carrier which binds with the matrix and releases in vivo the protein carrier, by cleaving from the enzymatic sites of the corresponding enzymes. It is confirmed that the peptide can be digested by plasmin in vitro. It＇s still yet to be confirmed whether this sequence can confer the protein that fuses with the characteristic which enables the binding with the extra-cellular matrix. The sequence was added at the C terminal of the GFP by Add-on PCR, then the fusion protein was expressed and purified. Results showed that the fusion GFP-containing protein provided the function of extra cellular matrix and heparin-sepharose CL-6B binding. Accordingly, the successful construction and purification of the fusion protein has laid a good foundation for the following-up of this study in vivo.