Abstract
Early examples of phage-display hbrarres were used to identify short, linear peptide eprtopes that could bind an antrbody or other target (1,2). Phage display offers a means not only to identify such peptides, but also to select high-affinity protein variants with improved affinity and specrftcity, by randomrzation of specrfrc residues within their binding eprtopes for receptors or other target molecules. Examples of such affinity- or specificity-improved proteins have included human growth hormone, zinc fingers, protease inhibitors, ANP., and antibodies (reviewed in 3,4). Since the btoactivity of such molecules is related to their fractional occupancy of a receptor or other binding target, higher-affinity and higher-specrficity variants have the potential to improve the effectiveness of and lower the dosage required for these molecules in therapeutic applications.
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© 1998 Humana Press Inc., Totowa, NJ
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Lowman, H.B. (1998). Phage Display of Peptide Libraries on Protein Scaffolds. In: Cabilly, S. (eds) Combinatorial Peptide Library Protocols. Methods in Molecular Biology™, vol 87. Humana Press. https://doi.org/10.1385/0-89603-392-9:249
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DOI: https://doi.org/10.1385/0-89603-392-9:249
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