National Centre for Biomolecular Research, Faculty of Science and CEITEC - Central European Institute of Technology, Masaryk University , Kamenice 5, 625 00 Brno-Bohunice, Czech Republic.
Langmuir. 2014 Feb 11;30(5):1304-10. doi: 10.1021/la402727a. Epub 2013 Sep 23.
Amphiphilic proteins and peptides can induce the formation of stable and metastable pores in membranes. Using coarse-grained simulations, we have studied the factors that affect structure of peptide-stabilized pores. Our simulations are able to reproduce the formation of the well-known barrel-stave or toroidal pores, but in addition, we find evidence for a novel "double-belt" pore structure: in this structure the peptides that coat the membrane pore are oriented parallel to the membrane plane. To check the predictions of our coarse-grained model, we have performed more detailed simulations, using the MARTINI force field. These simulations show that the double-belt structure is stable up to at least the microsecond time scale.
两亲性蛋白质和肽可以在膜中诱导形成稳定和亚稳的孔。使用粗粒化模拟，我们研究了影响肽稳定孔结构的因素。我们的模拟能够再现众所周知的桶状或环形孔的形成，但除此之外，我们还发现了一种新型“双带”孔结构的证据：在这种结构中，覆盖膜孔的肽与膜平面平行取向。为了检验我们的粗粒化模型的预测，我们使用 MARTINI 力场进行了更详细的模拟。这些模拟表明，双带结构至少在微秒时间尺度上是稳定的。
