Abstract
Bioorthogonal chemistry enables the interrogation of biomolecules and physiological processes that are inaccessible by using conventional research tools.1 A common experimental protocol starts by labeling a target biomolecule in cells or live organisms with a bioorthogonal functional group. Then, a probe molecule bearing complementary functionality is added to the system and the ensuing bioorthogonal chemical reaction delivers the probe specifically to the targets of interest. For many applications, rapid reaction kinetics are essential. This is particularly true for labeling experiments in live animals, in which reagent concentrations are limited (i.e., nm to low μm), or in which the process that is probed occurs on a fast time scale. Consequently, methodologists interested in the development of bioorthogonal reactions are increasingly focused on kinetic optimization.2
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