Ion channels are a large superfamily of membrane proteins that pass ions across membranes and are critical to diverse physiological functions in both excitable and nonexcitable cells and underlie many diseases. As a result, they are an important target class which is proven to be highly ''druggable''. According to our analysis, secondary structure and polarity play the major role in determining the drug-ion channels interactions activity. Secondary structure controls the membrane potential and interrogates ion channels in different conformational states. The drug-ion channels interaction needs gated state where they can switch conformation between a closed and an open state [42, 43] . Simulations on model nanopores reveal that a narrow hydrophobic region can form a functionally closed gate in the channel and can be opened by either a small increase in pore radius or an increase in polarity [107, 108] . Nowadays, intense research is being conducted to develop new drugs acting selectively on ion channel subtypes and aimed at the understanding of the intimate drug-channel interaction [109] .