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
T. Husslein et al., 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, FARADAY DIS, (111), 1998, pp. 201-208
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.