Silvestro L, Axelsen P H
Department of Pharmacology, Johnson Research Foundation for Molecular Biophysics, University of Pennsylvania, Philadelphia 19104-6084, USA.
Chem Phys Lipids. 1998 Nov;96(1-2):69-80. doi: 10.1016/s0009-3084(98)00081-4.
Cecropin A was examined in supported monolayer, bilayer, and multibilayer lipid membranes using attenuated total internal reflection Fourier-transform infrared spectroscopy. The spectral features provide an abundance of information about the conformation and orientation of the peptide, as well as about the effects of the peptide on lipid order. In this case, they serve to contrast results from the three preparations. The results of monolayer and bilayer studies are generally similar, although differences in the nature of the membranes appear to cause minor changes in the conformation and orientation of the peptide. The results of the multibilayer studies are different in many respects from those of the monolayer and bilayer studies, suggesting that fundamentally different peptide-lipid interactions occur in multibilayers.
使用衰减全内反射傅里叶变换红外光谱法,在支持的单层、双层和多层脂质膜中对杀菌肽A进行了检测。光谱特征提供了关于该肽的构象和取向以及该肽对脂质有序性影响的大量信息。在这种情况下,它们用于对比三种制剂的结果。单层和双层研究的结果通常相似,尽管膜性质的差异似乎会导致该肽的构象和取向发生微小变化。多层研究的结果在许多方面与单层和双层研究的结果不同,这表明在多层中发生了根本不同的肽-脂质相互作用。