| Abstract
| - 1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence ofbinding to the transmembrane peptide fragment of the influenza A M2 proton channel (M2TM)incorporated into 1,2-dimyristoyl-sn-glycero-3-phosphocholine liposomes. Above pH 7.5, whenM2TM bound the ligand, fluoroamantadine resonances became too broad to be detected.Fluoroamantadine interacted weakly with the liposomes, indicating it may first bind to thebilayer and then block target channels after diffusion across the membrane surface.
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