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Phage Display of Peptides in Ligand Selection for Use
in Affinity Chromatography
Joanne L. Casey, Andrew M. Coley, and Michael Foley
Summary
Large repertoires of peptides displayed on bacteriophage have been extensively used to
select for ligand-binding molecules. This is a relatively straightforward process involving
several cycles of selection against target molecules, and the resulting ligands can be
tailored to various applications. In this chapter we describe detailed methods to select
peptide ligands for affinity chromatography, with particular focus on selection of peptides
that mimic antigen epitopes. The selection process involves screening a phage peptide
library against a monoclonal antibody, proving the peptide is an authentic epitope mimic
and coupling the peptide mimotope to an affinity resin for purifying antibodies from
human serum. There are several other applications of phage peptides that could be used
for affinity chromatography; the approaches are outlined, but detailed methods have not
been included.
Key Words: Phage display; peptides; mimotopes; peptide ligands.
1. Introduction
Phage display of foreign peptides is an established technique now routinely
used in many laboratories since the pioneering work by Smith and colleagues 20
years ago (1). The flexibility and versatility of isolating peptides with affinity
for virtually any desired target has resulted in the growing use of random
peptide libraries for a wide variety of applications. Phage peptide libraries can
From: Methods in Molecular Biology, vol. 421: Affinity Chromatography: Methods and Protocols, Second Edition
Edited by: M. Zachariou © Humana Press, Totowa, NJ
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