We used steered molecular dynamics simulations to explore the hydrophobic barrier within the two pore domain potassium channel TWIK-1. This hydrophobic barrier is formed by Leucine 146 and Leucine 261 that lie below the selectivity filter on the cytoplasmic side of the protein. Experimental studies have shown that mutations of Leucine 146 and 261 allow more water to permeate to the selectivity filter and increase ion conduction (Nature Commun., 5, 4377, 2014). We use a collective variable (CV) that mimics tension by applying forces on lipids in the vicinity of the channel based on their proximity to explore the role of membrane interactions in modulating the hydrophobic barrier. Our group has studied the mechanosensitive channel of large conductance using a similar approach. By applying a harmonic potential to this CV, we observed different solvent accessibility to the selectivity filter. We found that TWIK-1 interacts strongly with lipids on the cytoplasmic side of the membrane through hydrogen bonding, which is higher compared to the periplasmic side. Positive amino acid residues Lysine (176, 275, 278) and Arginine (155, 162, 163, 171) alone contribute to one third of the hydrogen bond made by cytoplasmic side with protein. Furthermore, we explored the effects of mutating the hydrophobic L146 and L261 residues to Asparagine on solvent accessibility to the channel's selectivity filter and compare to the steered CV model.