Phages Displaying
Peptides with β Turn Conformation
LI Jia-Da,
TANG Wei-Gang, WANG Ke-Yi*
( Institute of Biochemistry and Cell Biology, Shanghai Institutes for
Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031 )
Abstract Peptide CX2GPX4C,
which was supposed to adopt a typical β turn conformation, was displayed on the
surface of filamentous phages by fusing to the N-terminus of minor coat protein
g3p. The diversity of this library was 1.04×108. Sequences from 19
randomly selected phage clones indicated that the distribution of nucleotides
and amino acids paralleled the expected frequency. The combined index of
hydropathy and isoelectric point of these 19 peptides were randomly distributed
over wide ranges. The enrichment was obtained after 3 rounds of screening with
monoclonal antibody 12CA5. And the results of phage ELISA and competitive ELISA
showed that the 15 individual phage clones randomly selected from the third
round elution specifically bound to the antigen binding site of the antibody.
This binding was abolished after destroying of the conformation.
Key words phage displayed peptide library； β turn
*Corresponding author： Tel, 86-21-64374430-5264； Fax, 86-21-64338357； e-mail, [email protected]