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In Situ Click Chemistry for the Identification of a Potent D-Amino Acid Oxidase Inhibitor トグチ, ショウヘイ トグチ, ショウヘイ Toguchi, Shohei ヒロセ, トモヤス ヒロセ, トモヤス Hirose, Tomoyasu 60116879 頼田, 和子 ヨリタ, カズコ Yorita, Kazuko 頼田 ヨリタ Yorita 和子 カズコ Kazuko 00175564 福井, 清 フクイ, キヨシ Fukui, Kiyoshi 福井 フクイ Fukui 清 キヨシ Kiyoshi Sharpless, K. Barry オオムラ, サトシ オオムラ, サトシ Ōmura, Satoshi スナヅカ, トシアキ スナヅカ, トシアキ Sunazuka, Toshiaki open access fragment-based lead discovery templated reaction ligand-binding site drug discovery triazole formation ligand affinity In situ click chemistry is a target-guided synthesis approach for discovering novel lead compounds by assembling organic azides and alkynes into triazoles inside the affinity site of target biogenic molecules such as proteins. We report in situ click chemistry screening with human D-amino acid oxidase (hDAO), which led to the identification of a more potent hDAO inhibitor. The hDAO inhibitors have chemotherapeutic potential as antipsychotic agents. The new inhibitor displayed competitive inhibition of hDAO and showed significantly increased inhibitory activity against hDAO compared with that of an anchor molecule of in situ click chemistry. The Pharmaceutical Society of Japan 2016-07-01 eng journal article VoR 314631 https://tokushima-u.repo.nii.ac.jp/records/2008359 https://doi.org/10.1248/cpb.c15-00867 10.1248/cpb.c15-00867 00092363 13475223 AA00602100 Chemical and Pharmaceutical Bulletin 64 7 695 703 https://tokushima-u.repo.nii.ac.jp/record/2008359/files/cpb_64_7_695.pdf application/pdf 1.41 MB 2020-11-12