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• W2090696823 endingPage "1857" @default.
• W2090696823 startingPage "1854" @default.
• W2090696823 abstract "Genetically encoded libraries of peptides and oligonucleotides are well suited for the identification of ligands for many macromolecules. A major drawback of these techniques is that the resultant ligands are subject to degradation by naturally occurring enzymes. Here, a method is described that uses a biologically encoded library for the identification of D-peptide ligands, which should be resistant to proteolytic degradation. In this approach, a protein is synthesized in the D-amino acid configuration and used to select peptides from a phage display library expressing random L-amino acid peptides. For reasons of symmetry, the mirror images of these phage-displayed peptides interact with the target protein of the natural handedness. The value of this approach was demonstrated by the identification of a cyclic D-peptide that interacts with the Src homology 3 domain of c- SRC. Nuclear magnetic resonance studies indicate that the binding site for this D-peptide partially overlaps the site for the physiological ligands of this domain." @default.
• W2090696823 created "2016-06-24" @default.
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• W2090696823 date "1996-03-29" @default.
• W2090696823 modified "2023-10-16" @default.
• W2090696823 title "Identification of <scp>d</scp> -Peptide Ligands Through Mirror-Image Phage Display" @default.
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• W2090696823 doi "https://doi.org/10.1126/science.271.5257.1854" @default.
• W2090696823 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8596952" @default.
• W2090696823 hasPublicationYear "1996" @default.
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