Molecular dynamics simulation of a hydrated diphytanol phosphatidylcholinelipid bilayer containing an alpha-helical bundle of four transmembrane domains of the Influenza A virus M2 protein

An alpha-helical bundle composed of four transmembrane portions of the M2 p rotein from the Influenza A virus has been studied ih a hydrated diphytanol phosphatidylcholine bilayer using molecular dynamic's (MD) calculations. E xperimentally, the sequence utilized is known to aggregate as a four-helix bundle and act as a pH-gated proton-selective ion channel, which is blocked by the drug amantadine hydrochloride. In the presented simulation, the ion channel was initially set up as a parallel four-helix bundle. The all-atom simulation consisted of almost 16 000 atoms, described classically, using a forcefield from the CHARMM22 database. Bilayers with and without the bund le were shown to be stable throughout the nanosecond timescale of the MD si mulation. Structural and dynamical properties of the bilayer both with and without the transmembrane protein are reported.