Development of a FUT8 Inhibitor with Cellular Inhibitory Properties

Yoshiyuki Manabe 1, Tomoyuki Takebe 1, Satomi Kasahara 1, Koki Hizume 1, Kazuya Kabayama 2, Yoshihiro Kamada 3, Akiko Asakura 4, Shinichiro Shinzaki 4, Shinji Takamatsu 5, Eiji Miyoshi 5, Ana García-García 6, Sergey Y Vakhrushev 7, Ramón Hurtado-Guerrero 6, Koichi Fukase 1. Angew Chem Int Ed Engl. 2024 Sep 28:e202414682. doi: 10.1002/anie.202414682.

Core fucosylation is catalyzed by α-1,6-fucosyltransferase (FUT8), which fucosylates the innermost GlcNAc of N-glycans. Given the association of FUT8 with various diseases including cancer, selective FUT8 inhibitors applicable to in vivo or cell-based systems are highly sought-after. Here, we report the discovery of a compound that selectively inhibits FUT8 in cell-based assays. High-throughput screening revealed a FUT8-inhibiting pharmacophore, and further structural optimization yielded an inhibitor with a KD of 49 nM. Notably, this binding occurs only in the presence of GDP (a product of the enzymatic reaction catalyzed by FUT8). Mechanistic studies suggested that this inhibitor generates a highly reactive naphthoquinone methide derivative at the binding site in FUT8, which subsequently reacts with FUT8. Furthermore, prodrug derivatization of this inhibitor improved its stability, enabling suppression of core fucose expression and subsequent EGFR and T-cell signaling in cell-based assays, paving the way for the development of drugs targeting core fucosylation.

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