Topology and dynamics of melittin within the liposome revealed by a combination of mass spectrometry and chemical modification.
Topology and dynamics of melittin within the liposome revealed by a combination of mass spectrometry and chemical modification.
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通过质谱和化学修饰的结合揭示了脂质体内蜂毒肽的拓扑结构和动力学。
DOI：
10.1016/j.bbrc.2010.04.020
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发表时间：
2010
影响因子：
3.1
通讯作者：
S. Izumi
中科院分区：
文献类型：
--
作者：
K. Saikusa;Y. Kono;S. Izumi
采用质谱联用技术研究了蜂毒肽在脂质体中的拓扑结构和动力学。MALDI-TOF MS和MALDI-QIT-TOF MS/MS分析表明，在脂质体存在下，蜂毒肽的四种伯胺均被完全快速乙酰化，但只有N-末端胺被乙酰化。这一结果表明蜂毒肽在脂质体内采用N端外跨膜拓扑结构。乙酰化的时间过程在任何检测的温度（6-30°C）下遵循一级动力学。反应速率常数小于水溶液中蜂毒肽乙酰化反应速率常数。乙酰化的活化能（74 kJmol −1）与脂质单体从膜上解离的活化能相当，表明蜂毒素在脂质体内的漂浮样纵向运动。这些结果表明，质谱结合化学修饰是非常有效的方式来澄清的拓扑结构和动态的肽结合到膜。
The topology and dynamics of melittin within the liposome were investigated by a mass spectrometry coupled with acetylation. The MALDI-TOF MS and MALDI-QIT-TOF MS/MS analyses revealed that only N-terminal amine of melittin was dominantly acetylated in the presence of liposome although all of four primary amines were completely and rapidly acetylated in aqueous solution. This result indicates that melittin adopts the N-terminal-outside transmembrane topology within the liposome. The time course of acetylation followed the first-order kinetics at any examined temperatures (6–30°C). The rate constant was less than that of the acetylation of melittin in aqueous solution. The activation energy for acetylation (74kJmol−1) was comparable to that for dissociation of a lipid monomer from the membrane, suggesting a float-like longitudinal motion of melittin within the liposome. These results demonstrate that a mass spectrometry combined with chemical modification is very efficient way for clarifying the topology and dynamics of peptides bound to the membrane.
影响因子：
3.4
作者：
Chen, FY;Lee, MT;Huang, HW
通讯作者：
Huang, HW
影响因子：
3.4
作者：
Yang, L;Harroun, TA;Huang, HW
通讯作者：
Huang, HW