Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces.
Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces.
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阿拉甲辛在磷脂/水和辛烷/水界面处的电压依赖性插入。
DOI：
10.1016/s0006-3495(01)76018-3
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发表时间：
2001
影响因子：
3.4
通讯作者：
M. Sansom
中科院分区：
文献类型：
--
作者：
D. Tieleman;H. Berendsen;M. Sansom
了解肽在脂质双层中的结合和插入是了解抗菌活性和膜蛋白折叠等现象的先决条件。我们描述了分子动力学模拟的抗菌肽丙甲菌素在脂质/水和辛烷/水的环境中，考虑到外部电场来模仿膜电位。在ATCIS正电位下，由于肽和脂质的缓慢动力学，丙甲霉素在10 ns的模拟中不会插入磷脂双层。然而，在辛烷N-末端插入发生在从0.33V/nm和更高的场强，在模拟高达100 ns的持续时间。丙甲霉素的插入分两步进行，对应于Gln 7侧链的去溶剂化，以及Aib 10和Gly 11的骨架。脯氨酸诱导的螺旋扭结角在插入过程中没有显着变化。聚丙氨酸和丙甲菌素在插入辛烷中和在水/辛烷界面处形成稳定的螺旋，在水/辛烷界面处，它们在相同的位置分配。在水中，多聚丙氨酸和丙甲菌素在多次模拟中部分展开。我们提出了一个详细的分析丙甲菌素插入到辛烷板和外部场对肽结构的影响。我们的研究结果提供了新的见解渠道形成的机制，丙甲霉素和膜相关螺旋的结构和动力学。
Understanding the binding and insertion of peptides in lipid bilayers is a prerequisite for understanding phenomena such as antimicrobial activity and membrane-protein folding. We describe molecular dynamics simulations of the antimicrobial peptide alamethicin in lipid/water and octane/water environments, taking into account an external electric field to mimic the membrane potential. Atcis-positive potentials, alamethicin does not insert into a phospholipid bilayer in 10ns of simulation, due to the slow dynamics of the peptide and lipids. However, in octane N-terminal insertion occurs at field strengths from 0.33V/nm and higher, in simulations of up to 100ns duration. Insertion of alamethicin occurs in two steps, corresponding to desolvation of the Gln7 side chain, and the backbone of Aib10 and Gly11. The proline induced helix kink angle does not change significantly during insertion. Polyalanine and alamethicin form stable helices both when inserted in octane and at the water/octane interface, where they partition in the same location. In water, both polyalanine and alamethicin partially unfold in multiple simulations. We present a detailed analysis of the insertion of alamethicin into the octane slab and the influence of the external field on the peptide structure. Our findings give new insight into the mechanism of channel formation by alamethicin and the structure and dynamics of membrane-associated helices.
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膜蛋白的核磁共振结构研究。
影响因子：
6.8
作者：
Marassi,FM;Opella,SJ
通讯作者：
Opella,SJ
影响因子：
3.4
作者：
Yili Wu;K. He;S. Ludtke;Huey W. Huang
通讯作者：
Yili Wu;K. He;S. Ludtke;Huey W. Huang
影响因子：
3.4
作者：
North, CL;BarrangerMathys, M;Cafiso, DS
通讯作者：
Cafiso, DS
DOI：
10.1016/s0304-4157(98)00021-5
发表时间：
1998-11-10
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON BIOMEMBRANES
影响因子：
--
作者：
White, SH;Wimley, WC
通讯作者：
Wimley, WC
影响因子：
56.9
作者：
Duan, Y;Kollman, PA
通讯作者：
Kollman, PA