Institute for Materials and Processes, School of Engineering, University of Edinburgh, Edinburgh, UK.
J Phys Chem B. 2010 Jan 21;114(2):826-39. doi: 10.1021/jp908320b.
In this article, we focus on several types of interactions between lipid membranes and alpha-helical peptides, based on the distribution of hydrophobic and hydrophilic residues along the helix. We employ a recently proposed coarse-grained model MARTINI and test its ability to capture diverse types of behavior. MARTINI provides useful insights on the formation of barrel-stave and toroidal pores and on the relation between these two mechanisms. Amphipathic nonspanning peptides are also described with sufficient accuracy. The picture is not as clear for fusion and transmembrane peptides. For each class of peptides, we calculate the potential of mean force (PMF) for peptide translocation across the lipid bilayer and demonstrate that each class has a distinct shape of PMF. The reliability of these calculations, as well as wider implications of the results, is discussed.
在本文中，我们基于沿螺旋分布的疏水和亲水残基，重点研究了几种脂质膜与α-螺旋肽之间的相互作用。我们采用了最近提出的粗粒化模型 MARTINI，并测试了它捕捉多种行为的能力。MARTINI 为桶状和环孔的形成以及这两种机制之间的关系提供了有用的见解。对于两亲性非贯穿肽，也可以进行足够准确的描述。对于融合和跨膜肽，情况就不那么清楚了。对于每一类肽，我们计算了肽穿过脂质双层的平均力势（PMF），并证明每一类肽的 PMF 形状都不同。我们讨论了这些计算的可靠性以及结果的更广泛影响。
