Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers

►In mechanically aligned lipid bilayers, the antimicrobial peptide Distinctin is absorbed on the membrane surface. ►The topology of distinctin does not change upon variation of lipid composition. ►Two different tilt angles were found for the two helical chains of distinctin, with chain 1 tilted by ~24 degrees, while chain 2 by ~5 degrees.