The interaction of amino-deuteromethylated melittin with phospholipid membranes studied by deuterium NMR.

Journal article

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.

Authors: Dempsey, C; Cryer, G; Watts, A

• Publication status: Published
• Journal: FEBS letters
• Volume: 218
• Issue: 1
• Pages: 173-177
• Publication date: 1987-06-01
• DOI: 10.1016/0014-5793(87)81041-4
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Chemistry, Physical; Phospholipids; Micelles; Melitten; Physicochemical Phenomena; Bee Venoms; Magnetic Resonance Spectroscopy; Deuterium; Dimyristoylphosphatidylcholine; Methylation; Erythrocyte Membrane; Lipid Bilayers