Unit

UNIT 17.4 Mapping Protein-Protein Interactions with Phage-Displayed Combinatorial Peptide Libraries

  1. Brian K. Kay1,
  2. Luisa Castagnoli2

Published Online: 1 FEB 2003

DOI: 10.1002/0471143030.cb1704s17

Current Protocols in Cell Biology

Current Protocols in Cell Biology

How to Cite

Kay, B. K. and Castagnoli, L. 2003. Mapping Protein-Protein Interactions with Phage-Displayed Combinatorial Peptide Libraries. Current Protocols in Cell Biology. 17:17.4:17.4.1–17.4.9.

Author Information

  1. 1

    Argonne National Laboratory, Argonne, Illinois

  2. 2

    University of Rome Tor Vergata, Rome, Italy

Publication History

  1. Published Online: 1 FEB 2003
  2. Published Print: JAN 2003

Abstract

This unit describes the process and analysis of affinity selecting bacteriophage M13 from libraries displaying combinatorial peptides fused to either a minor or major capsid protein. Direct affinity selection uses target protein bound to a microtiter plate followed by purification of selected phage by ELISA. Alternatively, there is a bead-based affinity selection method. These methods allow one to readily isolate peptide ligands that bind to a protein target of interest and use the consensus sequence to search proteomic databases for putative interacting proteins.