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Covalent drugs disrupt protein function by forming a specific bond between the drug and an amino acid residue on a target protein. Several important medicines produce a therapeutic response through a covalent mechanism of action (MOA). The renewed excitement for covalent drugs is motivated by distinct features of this class including high biochemical efficiency from non-equilibrium blockade of a target, pharmacological activity that can outlast drug pharmacokinetics, and access to challenging binding pockets on intractable protein targets. Our group developed sulfonyl-triazoles as a covalent binder of tyrosines to enable ligand discovery of catalytic and non-catalytic sites on proteins through sulfur-triazole exchange (SuTEx) chemistry. I will discuss efforts from my group and the field to advance the capabilities of SuTEx and related electrophiles for covalent ligand discovery by (i) facilitating the global discovery of actionable (i.e. high propensity for covalent binding) tyrosines in the human proteome using tandem liquid chromatography-mass spectrometry (LC-MS/MS) quantitative chemical proteomics, (ii) establishing a prioritization strategy to identify functional tyrosine sites based on reactive/structural features, (iii) demonstrating capabilities for tuning the reactivity and selectivity of sulfonyl-triazoles for a tyrosine site of interest using medicinal chemistry, (iv) providing a facile means for target identification in cell lysate and phenotypic screening formats, and (v) late stage functionalization of inhibitor compounds with a SuTEx reactive group for developing targeted covalent inhibitors.