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Updated: Aug 11, 2026
Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
[Isolation of a novel peptide that binds to BLyS from a 12-mer phage display peptide library]
Yan-Li Ding1, Wei Han, Qiong Shen
1School of Pharmaceutical Engineering, Shenyang Pharmaceutical University, Shenyang 110016, China. dingylding@yahoo.com.cn
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.
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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