Abstract
The expression of exogenous peptides on the surface of filamentous bacteriophage was initially described by Smith in 1985. Since his first study, different molecules such as small peptides and antibodies have been displayed on coat proteins of phage, greatly expanding the applications of the technology. The past decade has seen considerable progress in the techniques and applications of phage libraries. In addition, different screening methods have allowed isolation and characterization of peptides binding to several molecules in vitro, in the context of living cells, in animals and in humans. Here we review the applications, recent innovations, and future directions of phage display technology.
Highlights
Phage display technology was first introduced in 1985 by George Smith
Phage display allows the presentation of large peptide and protein libraries on the surface of filamentous phage, which leads to the selection of peptides and proteins, including antibodies, with high affinity and specificity to almost any target
Cardo-Vila et al introduced an approach based on phage display technology to identify molecules that interact with the cytoplasmic domain of the beta 5 integrin subunit
Summary
Phage display technology was first introduced in 1985 by George Smith. It was used as an expression vector, capable of presenting a foreign amino acid sequence accessible to binding an antibody. A large number of phage displayed peptide and protein libraries have been constructed (Bass et al 1990, McCafferty et al 1990, Barbas et al 1991, Smith 1991, Smith and Scott 1993, Hoogenboom 2002, Szardenings 2003), leading to various techniques for screening such libraries. Large peptide inserts of up to 38 amino acids can be introduced into the amino terminus of pIII protein without the loss of phage infectivity or particle assembly
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