OABK hydrochloride is a small-molecule switch that can be used to control protein activity.
A small-molecule switch for the activation of protein function through the site-specific incorporation of an ortho-azidobenzyloxycarbonyl lysine (OABK). The amino acid OABK is synthesized readily in three steps from 2-azidobenzyl alcohol via a succinimidyl carbonate. Deprotection results in the formation of lysine and, when OABK is incorporated into a protein, the formation of active wild-type protein. Genetically encoded OABK in conjunction with small-molecule activation allows for the conditional regulation of intracellular protein maturation. Incorporation of OABK (0.5 mM) at position K85 of EGFP inhibits fluorophore formation until the native lysine is generated through small-molecule activation (the model is based on Protein Data Bank (PDB). Introducing OABK at position K206 inhibits FLuc enzymatic activity by restricting the access of adenosine triphosphate (ATP) to the active site, until the enzyme is deprotected and activated through phosphine treatment. The incorporation of OABK into FLuc blocks the luciferase activity in the absence of small-molecule activation, as determined by a Bright-Glo luciferase assay[1].
[1]. Luo J, et al. Small-molecule control of protein function through Staudinger reduction. Nat Chem. 2016 Nov;8(11):1027-1034.