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. Author manuscript; available in PMC: 2023 Oct 21.
Published in final edited form as: ACS Chem Biol. 2022 Sep 29;17(10):2911–2922. doi: 10.1021/acschembio.2c00565

Figure 1:

Figure 1:

Current cyclic approaches for phage-displayed peptides and our proposed approach. A) Previous methods for the cyclization of two cysteines in phage-displayed peptides. R = H or peptide chain. B) The proposed novel cyclic linker CAmCBT that provides an asymmetric cyclization scaffold for phage display by selectively reacting with the N-terminal cysteine and then a proximity-driven reaction with an internal cysteine.