Journal of Microbiology

Research Support, Non-U.S. Gov't

Bacteria-Based In Vivo Peptide Library Screening Using Biopanning Approach: Ji-Hyeon Choi , Sang-Hyun Park; J. Microbiol. 2011;49(5):847-851. Published online November 9, 2011; DOI: https://doi.org/10.1007/s12275-011-1405-6

Abstract: Traditionally, library screening has been performed to identify biologically active agents including small molecules or peptides that inhibit target proteins or molecules with therapeutic interests. Due to its chemical nature, library screening is usually performed under in vitro environments using purified proteins and molecules. However, active agents identified from in vitro screenings often fail to exhibit biological activities in cells. To overcome this inherent limitation, we have developed an in vivo peptide library screening system that allows for the identification of dissociative inhibitors of protein interactions of interest. The screening is based on the reconstitution of the cI repressor from bacteriophage lambda with high-density expression peptide library and is entirely performed in bacteria cells. Furthermore, to enhance the efficacy and sensitivity of the screening, a multiple-round biopanning approach was employed for amplification and enrichment of positive peptides. Overall, this in vivo screening should provide a fast and efficient tool for identification of biologically active peptide molecules against target protein assembly.

Construction of a Hexapeptide Library using Phage Display for Bio-panning: Cho, Won Hee , Yoo, Seung Ku; J. Microbiol. 1999;37(2):97-101.

Abstract: Random hexapeptide library on the surface of filamentous bacteriophage was constructed using the SurfZAP vector. The size of the library was approximately 105. The peptide insert was flanked by two cysteines to constrain the peptide structure with a disulfide bond. This library was screened for the topoisomerase II binding peptide. Dramatic enrichment of the fusion phage over the VCS M13 helper phage was demonstrated by bio-panning affinity selection.

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