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- W4360952427 abstract "Abstract Tools for on‐demand protein activation enable impactful gain‐of‐function studies in biological settings. Thus far, however, proteins have been chemically caged at primarily Lys, Tyr, and Sec, typically through the genetic encoding of unnatural amino acids. Herein, we report that the preferential reactivity of diazo compounds with protonated acids can be used to expand this toolbox to solvent‐accessible carboxyl groups with an elevated p K a value. As a model protein, we employed lysozyme (Lyz), which has an active‐site Glu35 residue with a p K a value of 6.2. A diazo compound with a bioorthogonal self‐immolative handle esterified Glu35 selectively, inactivating Lyz. The hydrolytic activity of the caged Lyz on bacterial cell walls was restored with two small‐molecule triggers. The decaging was more efficient by small molecules than by esterases. This simple chemical strategy was also applied to a hemeprotein and an aspartyl protease, setting the stage for broad applicability." @default.
- W4360952427 created "2023-03-26" @default.
- W4360952427 creator A5014656935 @default.
- W4360952427 creator A5016811145 @default.
- W4360952427 creator A5042920686 @default.
- W4360952427 date "2023-04-25" @default.
- W4360952427 modified "2023-10-16" @default.
- W4360952427 title "Chemoselective Caging of Carboxyl Groups for On‐Demand Protein Activation with Small Molecules" @default.
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- W4360952427 doi "https://doi.org/10.1002/ange.202215614" @default.
- W4360952427 hasPublicationYear "2023" @default.
- W4360952427 type Work @default.