The ability to inhibit or modify enzyme function absent a catalytic pocket binding site target greatly expands the potentially druggable portion of the proteome. Furthermore, most classes of chimeric small molecules can act on many targets over their life cycle, lowering the effective dose compared to traditional inhibitors that act only on one protein at a time. These therapeutics provide an alternative mechanism of action that may be useful as a combination therapy in diseases where drug resistance is a concern. Chimeric drug activity is also highly dependent on distance between targeted proteins allowing effect to be effectively tuned through optimization of the linker structure.