Membrane curvature and surface area per lipid affect the conformation and oligomeric state of HIV-1 fusion peptide: A combined FTIR and MD simulation study
Membrane curvature and surface area per lipid affect the conformation and oligomeric state of HIV-1 fusion peptide: A combined FTIR and MD simulation study
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DOI：
10.1016/j.bbamem.2007.11.014
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发表时间：
2008-04-01
影响因子：
3.4
通讯作者：
Kosztin, Ioan
中科院分区：
文献类型：
--
作者：
Barz, Bogdan;Wong, Tuck C.;Kosztin, Ioan
傅里叶变换红外光谱（FTIR）和分子动力学（MD）模拟结果支持我们的假设，即HIV-1 gp41融合结构域或融合肽（gp41- fp）的构象和寡聚状态是由膜曲率影响的每脂质膜表面积（APL）决定的。气溶胶- ot （AOT）反胶束体系中gp41-FP的FTIR表明，随着AOT/水比的变化，APL从50埃降低到35埃(2)，FP由单体α -螺旋结构转变为低聚p-片结构。在POPE脂质双分子层体系中的MD模拟表明，当施加负表面张力降低APL时，螺旋单体开始展开成轮状结构。此外，在非平衡MD模拟过程中，施加侧压力的增加有利于β -片结构的形成。这些结果提供了更好地了解gp41-FP结构与膜之间的关系，这对理解膜融合过程至关重要。本研究结果对HIV-1 FP的融合原性结构的意义进行了讨论。(c) 2007 Elsevier B.V.版权所有
Fourier-transformed infrared spectroscopy (FTIR) and molecular dynamics (MD) simulation results are presented to support our hypothesis that the conformation and the oligomeric state of the HIV-1 gp41 fusion domain or fusion peptide (gp41-FP) are determined by the membrane surface area per lipid (APL), which is affected by the membrane curvature. FTIR of the gp41-FP in the Aerosol-OT (AOT) reversed micellar system showed that as APL decreases from similar to 50 to 35 angstrom(2) by varying the AOT/water ratio, the FP changes from the monomeric alpha-helical to the oligomeric p-sheet structure. MD simulations in POPE lipid bilayer systems showed that as the APL decreases by applying a negative surface tension, helical monomers start to unfold into turn-like structures. Furthermore, an increase in the applied lateral pressure during nonequilibrium MD simulations favored the formation of beta-sheet structure. These results provide better insight into the relationship between the structures of the gp41-FP and the membrane, which is essential in understanding the membrane fusion process. The implication of the results of this work on what is the fusogenic structure of the HIV-1 FP is discussed. (c) 2007 Elsevier B.V. All rights reserved.