Phage display describes a selection technique in which a library of peptide or protein variants is expressed on the outside of a phage virion, while the genetic material encoding each variant resides on the inside (1-3). This creates a physical linkage between each variant protein sequence and the DNA encoding it, which allows rapid partitioning based on binding affinity to a given target molecule (antibodies, enzymes, cell-surface receptors, etc.) by an in vitro selection process called panning (4). In its simplest form, panning is carried out by incubating a library of phage-displayed peptides on a plate (or bead) coated with the target, washing away the unbound phage, and eluting the specifically bound phage (Figure 1). The eluted phage are then amplified and taken through additional binding/amplification cycles to enrich the pool in favor of binding sequences. After 3–4 rounds, individual clones are characterized by DNA sequencing and binding assays.
The Ph.D.-7 Phage Display Peptide Library Kit v2 is based on a combinatorial library of random heptapeptides fused to the N-terminus of a minor coat protein (pIII) of M13 phage (5-9). The peptide is followed by a short spacer (Gly-Gly-Gly) which directly precedes the wild-type pIII sequence. The library consists of ~109 electroporated sequences amplified once to yield approximately 100 copies of each sequence in 10 μl of the supplied phage.
Displayed Peptide Form: X7-GGG-native M13 pIII
Figure 1: Panning with a pentavalent peptide library displayed on pIII.
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