<p>Protons are crucial for biological energy transduction between membrane proteins. While experiments suggest rapid proton motion over large distances at the membrane-water interface, computational studies employing a single excess proton found the proton immobilized near the lipid headgroup. To address this discrepancy, we conduct DFTB3 simulations by incrementally adding protons up to three. We show that a single proton moves rapidly toward the nearest headgroup, where it is either repelled by a choline group or binds covalently to phosphatic oxygen. With multiple protons, while some are trapped by the lipid headgroups, the remaining proton diffuses laterally faster than in bulk water. Driven by excess energy, this proton initially jumps to the center of the water slab before relaxing into the third- and second-hydration shells. Lateral diffusion rates increase as the proton stabilizes in the second hydration shell. These results provide insights into proton dynamics near membranes and explain experimental observations.</p>