Phage-displayed peptide libraries

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Abstract

Over the past year, significant advances have been achieved through the use of phage-displayed peptide libraries. A wide variety of bioactive molecules, including antibodies, receptors and enzymes, have selected high-affinity and/or highly-specific peptide ligands from a number of different types of peptide library. The demonstrated therapeutic potential of some of these peptides, as well as new insights into protein structure and function that peptide ligands have provided, highlight the progress made within this rapidly-expanding field.

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      As compared to larger molecules such as proteins, the advantages of peptides are their lower immunogeneicity and cost of synthesis, easier diffusion towards targeted sites, as well as their greater in vivo stability. Phage display technology is one of the most frequently used screening tools for the identification of peptide ligands able to target any type of biomolecules (Smith and Petrenko, 1997; Zwick et al., 1998). This technique consists in the insertion of a foreign DNA fragment (oligonucleotide) in the structural gene of bacteriophages, which leads to the expression of a peptide at the surface of the viral particle.

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