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Here, we introduce a lysine\u2010selective and proximity\u2010induced photocyclization platform enabled by the noncanonical amino acid\n                    <jats:italic>o<\/jats:italic>\n                    \u2010nitrobenzyl alcohol lysine (\n                    <jats:italic>o<\/jats:italic>\n                    \u2010NBAK), incorporated into phage\u2010displayed peptides and activated using the mild and fully biocompatible PANAC photoclick reaction. Photocyclization proceeded efficiently on both purified pIII fusion proteins and intact phage particles with no detectable loss of infectivity, driven by intramolecular proximity between\n                    <jats:italic>o<\/jats:italic>\n                    \u2010NBAK and a neighboring lysine, yielding well\u2010defined stable indazolone macrocycles. Screening PANAC\u2010cyclized libraries against disease\u2010relevant proteins produced cyclic ligands with nanomolar to low\u2010micromolar affinities, and cyclization enhanced proteolytic stability by more than an order of magnitude. These findings establish the first lysine\u2010selective cyclic peptide library constructed on phage through ncAA incorporation and demonstrate a robust, chemoselective, and broadly applicable strategy for discovering bioactive cyclic peptides.\n                  <\/jats:p>","DOI":"10.1002\/anie.3703404","type":"journal-article","created":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T11:27:15Z","timestamp":1783596435000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Genetically Encoded Lysine\u2010Selective Photocyclization Enables Phage Display Selection of Cyclic Peptide Binders"],"prefix":"10.1002","volume":"65","author":[{"given":"Xiao\u2010Qin","family":"Yang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Natural Product Chemistry, Lanzhou Magnetic Resonance Center, College of Chemistry and Chemical Engineering Lanzhou University  Lanzhou P. R. 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