title: Phages Displaying Peptides with beta Turn Conformation.
abstract: Peptide CX(2)GPX(4)C, which was supposed to adopt a typical beta 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 1.04x10(8). 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.
authors.affiliation: Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China. kyw0717@sunm.shcnc.ac.cn
authors.forename: Jia-Da
authors.initials: JD
authors.lastname: Li
authors.forename: Wei-Gang
authors.initials: WG
authors.lastname: Tang
authors.forename: Ke-Yi
authors.initials: KY
authors.lastname: Wang