Journal of South China University of Technology (Natural Science Edition) ›› 2005, Vol. 33 ›› Issue (10): 90-94.

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Design of Recombined Angiotensin-Converting Enzyme Inhibitor Peptide Sequence and Construction of Expression System

Liu Dong1  Li Shi-min2  Zhang Li-jun2  Tang Yu-qian1  Liang Shi-zhong1   

  1. 1.College of Biological Science and Engineering,South China Univ.of Tech.,Guangzhou 510640,Guangdong,China;2.School of Applied Chemistry and Biological Technology,Shenzhen Polytechnic,Shenzhen 518055,Guangdong,China
  • Received:2004-12-08 Online:2005-10-25 Published:2005-10-25
  • Contact: 刘冬(1968-)，男，博士生，深圳职业技术学院 副教授，主要从事生物技术方面的研究 E-mail:liudongsz@oa.szpt.net
  • About author:刘冬(1968-)，男，博士生，深圳职业技术学院 副教授，主要从事生物技术方面的研究
  • Supported by:

    广东省社会发展攻关资助项目(20032979)；深圳市科技计划资助项目(03KJ6021)

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Abstract:

Five angiotensin-converting enzyme inhibitor peptide(ACEIP)sequences were first designed and synthesized according to the relationship between the function and the structure of ACEIP.Next,the optimal peptide,namely,P3(six-amino-acid sequence)was determined by the bioactivity measurement and the digesting test in vitro.It was then jointed at the specific enzyme cleavage site to construct a six-copy fusion peptide.The corresponding coding gene was cloned into pGEX4T-2.The fusion expression vector of pGEX4T-2-ACEIP was finally transformed into Escherichia coli BL21.The results of the double enzyme-cleavage,PCR an d the sequence analysis all indicate that the recombinant plasmid pGEX-T-2-ACEIP is successfully constructed.

Key words: angiotensin-converting enzyme inhibitor peptide, sequence design, gene recombination