Ion channels are involved in many cellular mechanisms, and cellular excitability is one of the most critical. Most of the potassium channels allow the efflux of the potassium ions, leading to the repolarization of the cell. The voltage-gated potassium channel Kv7 family (also known as KCNQ) has five members. Mutations of these channels cause serious, sometimes fatal, disorders such as epilepsies, cardiac arrhythmias and muscular paralysis. In this regard, Kv7s represent potential pharmacological targets for such conditions. Unfortunately, no one has been able to generate effective drugs that target these channels without side-effects. Thus, the big challenge is developing drug molecules that can differentiate between closely related Kv channels, thereby causing minimal side-effects. In recent years, a compound called MaxiPost (BMS-204352) has been shown to be both a negative modulator of the Kv7.1 channel and a positive modulator of the Kv7.4 and Kv7.5 channels, while not showing any significant effect on the canonical M-channel Kv7.2/Kv7.3. On the contrary, its R-enantiomer strongly inhibited the Kv7.4 and Kv7.5 activities. The different modulation carried out by this drug on the different Kv7 members, and the reversal of the effect in the case of its R-enantiomer, suggest that a possible explanation could lie in the structural differences of the Kv7 channels. Experimental evidence suggests that MaxiPost binds at the same pocket where the well-known modulator retigabine binds. In fact, mutation of Trp242 in Kv7.4 has been shown to abolish the activation effect of both MaxiPost and retigabine. To verify this hypothesis, we performed molecular docking of MaxiPost focused on the known retigabine binding site. We aim now to evaluate the stability and reliability of the best docking poses with molecular dynamics (MD) simulations, embedding the protein and the ligand in a bilayer phospholipid membrane.