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. 2020 Apr 8;142(18):8367–8373. doi: 10.1021/jacs.0c01879

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Copyright © 2020 American Chemical Society

This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.

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Phage display of bicyclic peptides¹² for affinity selection of G4 ligands. Bacteriophages express libraries of peptides with cysteines at defined positions on their coat proteins (AG, X = any of the 20 canonical amino acids, n = 3 or 4 in this study). These Cys-rich libraries are bicyclized quantitatively by 1,3,5-tris(bromomethyl)benzene in situ. G4 ligands are selected from this bicyclic peptide library (around 10⁸ – 10⁹ members) by presenting biotinylated G4 targets for capture.

Inline graphic — Phage display of bicyclic peptides¹² for affinity selection of G4 ligands. Bacteriophages express libraries of peptides with cysteines at defined positions on their coat proteins (AG, X = any of the 20 canonical amino acids, n = 3 or 4 in this study). These Cys-rich libraries are bicyclized quantitatively by 1,3,5-tris(bromomethyl)benzene in situ. G4 ligands are selected from this bicyclic peptide library (around 10⁸ – 10⁹ members) by presenting biotinylated G4 targets for capture.