Statins exert their primary mechanism of action through inhibition of HMG-CoA reductase, thereby preventing cholesterol synthesis. Additionally, statins have many, so called “pleotropic”, effects that are independent of HMG-CoA reductase inhibition. Because statins are amphiphiles that modulate the function of different, structurally unrelated membrane proteins, we explored whether statins could alter lipid bilayer mechanical properties at the concentrations where they alter membrane protein function. To this end, we used a gramicidin-based fluorescence quench method as well as single-channel electrophysiology. We found that atorvastatin, fluvastatin, lovastatin, mevastatin, pravastatin, and simvastatin increase the rate of fluorescence quenching, meaning that they shift the gA monomer ↔ dimer equilibrium toward the conducting dimers. Statins thus alter bilayer mechanical properties, with fluvastatin being the most active and rosuvastatin the least active. When examined electrophysiologically, simvastatin, pravastatin, and fluvastatin increase the lifetime and appearance rate of channels formed by both short (13-residue) and long (15-residue) gramicidin analogues, with fluvastatin being the most active and pravastain being the least active. The changes in gA channel function depend on the channel-bilayer hydrophobic mismatch, as we observe the larger effects on the shorter channels; the channels with the larger hydrophobic mismatch. We conclude that statins alter lipid bilayer properties by a common mechanism, through an increase in bilayer elasticity, and that specific channel-statin interactions are not involved.