Department of Biochemistry, University of Oxford, South Parks Rd, Oxford OX1 3QU, UK.
Eur Biophys J. 2010 Oct;39(11):1537-45. doi: 10.1007/s00249-010-0611-1. Epub 2010 May 25.
The oblique insertion of type 1 viral fusion peptides into the cell membrane of the host cell has been shown previously to be an essential element of viral fusion. The actual physical explanation of the cause of the oblique insertion has been the subject of speculation. In this study the physical properties of the fusion peptide surface have been determined computationally and compared to the tilt angles determined both experimentally and by the use of molecular dynamics. It has been shown that the relationship between the distribution of lipophilic potential over the peptide surface and the peptide geometry control the tilt angle of the peptide in a biomimetic DMPC bilayer whereas the depth of penetration into the bilayer appears to be determined by the electrostatic potential and hydrogen bonding at the C-terminus.
先前的研究表明，I 型病毒融合肽斜向插入宿主细胞膜是病毒融合的必要条件。至于导致这种斜向插入的实际物理原因，一直以来都只是推测。在这项研究中，我们通过计算的方法确定了融合肽表面的物理特性，并与实验和分子动力学确定的倾斜角度进行了比较。结果表明，在仿生 DMPC 双层膜中，肽表面的疏水性势能分布与肽几何形状之间的关系控制着肽的倾斜角度，而肽在双层膜中的穿透深度似乎取决于 C 末端的静电势和氢键。
