Biological probes play an important role in the advancement of biochemistry, chemical biology, and medicine. Molecular targeting probes can elucidate biological mechanisms by binding to a target molecule in a way that disrupts its biological function. Molecular probes can selectively label a cellular organelle or protein which assists in biological studies. The development of new molecular targeting probes is critical for the progression of biosciences. Methods for quickly developing potent molecular targeting probes are still needed. A molecular targeting probe recognizes its target through strong intermolecular binding interactions. Early small molecule probes targeted deep hydrophobic binding pockets. Unfortunately, only a small portion of the biomolecules in the human genome can be targeted this way. As an alternative, proteins and peptides have been developed as probes and therapeutics for extracellular molecular targets. However, theses alternative methods are not always amenable for intracellular molecular targeting. Therefore, there remains a class of intracellular signaling proteins, such as STAT3, that signal through shallow hydrophilic binding interfaces. These large binding interfaces usually do not bind well with hydrophobic small molecules, because these have evolved to interact with other intracellular proteins. Previous studies have shown that Rh(II) can enhance small molecule-probe binding thereby increasing the probes efficacy. However, this phenomenon had only been demonstrated in simple protein-ligand assays.