Journal of South China University of Technology (Natural Science Edition) ›› 2006, Vol. 34 ›› Issue (5): 72-75,126.

• Biology Science • Previous Articles     Next Articles

Stability of Basic Fibroblast Growth Factor with Acid-Induced Site-Directed Mctor with Am ino tation

Xie Qiu-ling  Zhang Ling  Hong An   

  1. 1.Bioengineering Institute of Jinan Univ.,Guangzhou 5 10632,Guangdong,China;2.Key Laboratory of Bioengineering Medicine of Guangdong Province,Guangzhou 510632,Guangdong,China
  • Received:2005-03-06 Online:2006-05-25 Published:2006-05-25
  • Contact: 谢秋玲(1968-)，女，副研究员，主要从事基因工程药物研究 E-mail:txql@jnu.edu.cn
  • About author:谢秋玲(1968-)，女，副研究员，主要从事基因工程药物研究
  • Supported by:

    国家“十五”重大科技专项项日(2002AA2Z3344)

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Abstract:

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 investi-gation into the electrostatic potential distribution and the solvent.accessible surface area of two bFGF protein mono.mers.The results indicate that the bioactivity and heparin afinity 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 Cys78 and Cys 96 mutation plays an important role in the covalent interaction of hbFGF but has no obvious
effect on the non.covalent interaction.

Key words: basic fibroblast growth factor, stability, amino acid, site-directed mutation, electrostatic interaction, hydrophobic interaction