Voltage-gated K+ channels are widely expressed controllers of cellular behavior. Each channel has a gate between the cytosol and its K+ conductive pore to control the flow of potassium. Small molecules that enter through this gate can block the pore. The interface between a channel and its blocker may change during pore closure, producing channel-state-biased blocker affinity or, equivalently, bias of channel state by bound blockers. My findings suggest that RY785, a small molecule which inhibits KV2.1 voltage-gated K+ channels, enters through the cytosolic gate and has biased affinity for closed channels. KV2.1 channels may include KV8.1 subunits which affect the structure and gating of the pore. I also find that RY785 exhibits a similar mechanism of inhibition for KV2.1/KV8.1 channels but with much lower affinity. Interestingly, the voltage dependence of RY785 inhibition suggests opening the cytosolic gate of KV2.1 is not sufficient to permit K+ conduction and that heteromerization with KV8.1 reduces closure of this gate.In addition to my work on potassium channel pharmacology, I include as an appendix a reflection on my experience designing and teaching an undergraduate seminar on modern ion channel research. This reflection was composed in partial satisfaction of the requirements for obtaining a graduate academic certificate in undergraduate education. This scholarly effort yielded proof-of-concept that undergraduate students benefit from instruction on how to locate and analyze original scientific research articles and produced template instructional materials.