氨基酸定点突变碱性成纤维生长因子的稳定性  

Stability of Basic Fibroblast Growth Factor with Amino Acid-Induced Site-Directed Mutation

作　　者：谢秋玲[1] 张玲[1] 洪岸[2] 

机构地区：[1]暨南大学生物工程研究所,广东广州510632 [2]暨南大学广东省生物工程药物重点实验室,广东广州510632

出　　处：《华南理工大学学报（自然科学版）》2006年第5期72-75,126,共5页Journal of South China University of Technology(Natural Science Edition)

基　　金：国家"十五"重大科技专项项目(2002AA2Z3344)

摘　　要：为了提高碱性成纤维生长因子的体外稳定性,分析比较了野生型人碱性成纤维细胞生长因子(hbFGF)和半胱氨酸(Cys)定点突变型hbFGF的生物活性、肝素结合能力、体外聚合程度和聚合成分,以及两种蛋白单体的表面静电分布和溶剂可及表面面积.结果表明,突变型hbFGF保持了野生型hbFGF的生物活性以及肝素结合能力,并显著了降低了体外聚合程度,而单体三维结构中的静电分布和溶剂可及表面面积变化不明显.由此可见,Cys突变影响了hbFGF的共价聚合,而对非共价聚合影响不大.In order to improve the stability of basic fibroblast growth＇ factor （bFGF） in vitro, the bioactivity, the heparin affinity, the aggregation degree and the corresponding aggregation component in wild human bFGF （hb FGF） and its mutant whose Cys78 and Cys 96 mutated to Ser were analyzed and compared, followed by the investigation into the electrostatic potential distribution and the solvent-accessible surface area of two bFGF protein monomers. The results indicate that the bioactivity and heparin affinity of the mutated hbFGF keep constant while the aggregation degree of the mutated bFGF in vitro decreases although the electrostatic potential distribution and solvent-accessible surface area of hbFGF mutant dimer are similar to those of wild hbFGF dimer. All these reveal that the CysT8 and Cys 96 mutation plays an important role in the covalent interaction of hbFGF but has no obvious effect on the non-covalent interaction.

关 键 词：碱性成纤维细胞生长因子 稳定性 氨基酸 定点突变 静电作用 疏水相互作用 

分 类 号：Q518.4[生物学—生物化学]