The interaction of amino-deuteromethylated melittin with phospholipid membranes studied by deuterium NMR.
Melittin, deuteromethylated on each of the four amino groups (Gly-1 N alpha and Lys-7, 21, and 23 N epsilon), was prepared by reductive methylation using deuteroformaldehyde and NaBD3CN. Deuterium NMR spectra were obtained for the modified peptide (D-melittin) bound to phospholipid bilayers and erythrocyte ghosts. D-Melittin at 4 mol% (peptide:lipid) induced reversible transitions between extended bilayers and micelles at the phase-transition temperature in dimyristoylphosphatidylcholine (DMPC) bilayers. These changes in lipid morphology did not occur at 1 mol% D-melittin: DMPC and the peptide was highly motionally restricted in gel in gel-phase lipid.
D001514:Bee Venoms; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003903:Deuterium; D004134:Dimyristoylphosphatidylcholine; D004910:Erythrocyte Membrane / Q000187:drug effects*; D008051:Lipid Bilayers / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D008555:Melitten / Q000031:analogs & derivatives* / Q000494:pharmacology; D008745:Methylation; D008823:Micelles; D010743:Phospholipids / Q000378:metabolism*
D001514:Bee Venoms; D008051:Lipid Bilayers; D008823:Micelles; D010743:Phospholipids; D008555:Melitten; D003903:Deuterium; D004134:Dimyristoylphosphatidylcholine