Dempsey C E, Cryer G D, Watts A
FEBS Lett. 1987 Jun 22;218(1):173-7. doi: 10.1016/0014-5793(87)81041-4.
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.
蜂毒肽在四个氨基（甘氨酸-1的Nα以及赖氨酸-7、21和23的Nε）上均进行了氘代甲基化，通过使用氘代甲醛和NaBD3CN进行还原甲基化反应制备而成。获得了与磷脂双层和红细胞影结合的修饰肽（氘代蜂毒肽）的氘核磁共振谱。在二肉豆蔻酰磷脂酰胆碱（DMPC）双层中，4摩尔％（肽：脂质）的氘代蜂毒肽在相变温度下诱导了伸展双层和胶束之间的可逆转变。在1摩尔％的氘代蜂毒肽：DMPC时未发生脂质形态的这些变化，并且该肽在凝胶相脂质的凝胶中运动受到高度限制。
