The M2 protein is an integral part of the viral membrane of influenza A virus that conducts protons across the membrane to acidify the viral interior. NMR and X-ray diffraction measurements show that M2 alters its conformation as the pH is reduced which is correlated with its ability to transport protons. 2D IR experiments probe the water in the channel, and have revealed a pH dependent change in the dynamical properties through spectral densities of isotopically labeled amide modes. We have utilized the aforementioned 2D IR spectral signatures of water to probe the effects of drug binding inside the channel. Spectral dynamics are invariant to drug binding, indicating that the channel water plays a stabilizing role to drugs. 2D IR experiments also reveal multiple conformations of the channel upon drug binding, possibly from different orientations of the drug molecule in the channel.

Spectral densities of amide modes probe effects of drug binding on water in the M2 channel

244th National Meeting (2012)

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