Conformation of the gramicidin A channel in phospholipid vesicles: fluorine-19 nuclear magnetic resonance study

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Abstract
The membrane conformation of the peptide ionophore gramicidin A is shown by 119F NMR to be described by the N-terminal to N-terminal .beta.LD helical dimer model proposed by Urry. Fully active analogs of gramicidin with 19F labels at both the N-and C-termini are prepared synthetically. Labeled peptides are incorporated into small unilamellar vesicles of dimyristoylphosphatidylcholine. Measurements of the accessibility of the labels to either aqueous or lipophilic paramagnetic probes show that the N-terminus of gramicidin is located in the membrane interior and the C-terminus is at the membrane surface. Of the specific models proposed for the structure of gramicidin, these data are consistent only with that of Urry. The C-terminal 19F NMR peak in vesicles actually consists of 3 overlapping peaks. Experiments with the aqueous shift reagent Tm3+ show that C-terminal 19F nuclei in the inner and in the outer leaflets of vesicles resonate at different frequencies. The outer leaflet peak in turn consists of 2 overlapping peaks, possibly due to a local rearrangement of the C-terminal label.