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

FEBS Letters

Watts, Anthony¹  Cryer, Geoff D.¹  Dempsey, Christopher E.¹ 

[1] Biochemistry Dept, Oxford University, South Parks Rd, Oxford OX1 3QU, England

关键词: Melittin;    Deuteration;    2H-NMR;    Phospholipid membrane;    Vesicle-melittin transition;    Chain melting;    DMPC;    dimyristoylphosphatidylcholine;    DPPC;    dipalmitoylphosphatidylcholine;    PL;    phospholipase;    PS;    phosphatidylserine;    T m;    gel-liquid crystalline phase transition temperature;   

DOI  :  10.1016/0014-5793(87)81041-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Melittin, deuteromethylated on each of the four amino groups (Gly-1 Nα and Lys-7, 21, and 23 Nε), 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-phase lipid.

【 授权许可】

Unknown