Abstract
The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We have obtained residue-specific environmental parameters in the presence of the antiviral drug amantadine to gain information about the drug bound state of M2 in POPC/POPG lipid bilayers. Power saturation studies of spin-labeled peptides reconstituted in a DOGS-NTA(Ni)-containing bilayers report on the accessibility of spin labels to nickel(II) chelated at the aqueous-lipid interface.
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