遗传 ›› 2006, Vol. 28 ›› Issue (2): 208-211.

• 研究报告 • 上一篇    下一篇

BLyS对噬菌体随机12肽库的筛选

丁艳丽1;2 ; 韩 威1;2 ; 沈 琼2 ; 刘 惠2 ; 杨胜利1;2 ; 龚 毅2   

  1.  1. 沈阳药科大学制药工程学院,沈阳 110016; 2. 中国科学院上海生命科学研究院,上海 200233
  • 收稿日期:2005-01-19 修回日期:2005-05-24 出版日期:2006-02-10 发布日期:2006-02-10
  • 通讯作者: 龚毅

Isolation of A Novel Peptide That Binds to BLyS from a 12-mer Phage Display Peptide Library

DING Yan-Li1,2 , HAN Wei1,2 , SHEN Qiong2 , LIU Hui2 , YANG Sheng-Li1,2,

  1. 1. School of Pharmaceutical Engineering, Shenyang Pharmaceutical University, Shenyang 110016,China;2. Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200233,China
  • Received:2005-01-19 Revised:2005-05-24 Online:2006-02-10 Published:2006-02-10
  • Contact: GONG Yi

摘要:

 用B淋巴细胞刺激因子(BLyS)对噬菌体随机12肽库进行亲和淘洗,3轮筛选后阳性噬菌体得到富集。用ELISA鉴定噬菌体克隆,多个阳性克隆测序后得到了同一个小肽序列(RHKIQLRQNIIT)。将该小肽与GST融合,在大肠杆菌中进行表达及纯化,ELISA实验进一步验证了其具有与BLyS特异结合的活性。该小肽有可能成为其天然受体的拮抗剂。
 
 
 
 
 
 
 
 
 

关键词: 小肽, 表达, 噬菌体肽库, BLyS

Abstract: A 12-mer phage display peptide library was screened for specific binders against B lymphocyte stimulator (BLyS). After 3 rounds of panning, positive phage clones were enriched. ELISAs were used to identify positive phages, and the DNA encoding the positive peptide (RHKIQLRQNIIT) was cloned and expressed as a GST fusion protein in E. coli. After purification, the identity of the fusion protein was confirmed through its specific binding to BLyS by ELISA. We have obtained a peptide that can bind to BLyS and probably act as an antagonistic peptide against the natural BLyS receptor.

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