Cornell B A, Weir L E, Separovic F
CSIRO Division of Food Research, North Ryde, NSW, Australia.
Eur Biophys J. 1988;16(2):113-9. doi: 10.1007/BF00255521.
The helical polypeptide, gramicidin A has been widely studied as a model for the interactions of hydrophobic proteins with lipid bilayer membranes. Many reports are now available of the physical effects of mixing gramicidin A with phospholipid membranes, however, the interpretation of these data remains unclear. The purpose of this communication is to examine the controversial claim that high concentrations of gramicidin A' cause disorder within the L alpha phase of phosphatidylcholine-water dispersions. Solid-state nuclear magnetic resonance (NMR), density gradient and X-ray diffraction techniques are used to confirm the existence of such an effect and mechanisms are discussed which account for the known effects of gramicidin A on lipid bilayers.
螺旋多肽短杆菌肽A作为疏水蛋白与脂质双分子层膜相互作用的模型已得到广泛研究。现在有许多关于短杆菌肽A与磷脂膜混合后的物理效应的报道,然而,这些数据的解释仍不明确。本通讯的目的是检验一个有争议的说法,即高浓度的短杆菌肽A会导致磷脂酰胆碱-水分散体系的Lα相内出现无序状态。使用固态核磁共振(NMR)、密度梯度和X射线衍射技术来证实这种效应的存在,并讨论了一些机制,这些机制解释了短杆菌肽A对脂质双层的已知效应。