两亲性抗菌肽在磁场定向脂质双层中的分布。
Amphipathic antimicrobial piscidin in magnetically aligned lipid bilayers.
机构信息
Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California, USA.
出版信息
Biophys J. 2011 Sep 7;101(5):1086-94. doi: 10.1016/j.bpj.2011.07.015.
Abstract
The amphipathic antimicrobial peptide piscidin 1 was studied in magnetically aligned phospholipid bilayers by oriented-sample solid-state NMR spectroscopy. (31)P NMR and double-resonance (1)H/(15)N NMR experiments performed between 25 °C and 61 °C enabled the lipid headgroups as well as the peptide amide sites to be monitored over a range of temperatures. The α-helical peptide dramatically affects the phase behavior and structure of anionic bilayers but not those of zwitterionic bilayers. Piscidin 1 stabilizes anionic bilayers, which remain well aligned up to 61 °C when piscidin 1 is on the membrane surface. Two-dimensional separated-local-field experiments show that the tilt angle of the peptide is 80 ± 5°, in agreement with previous results on mechanically aligned bilayers. The peptide undergoes fast rotational diffusion about the bilayer normal under these conditions, and these studies demonstrate that magnetically aligned bilayers are well suited for structural studies of amphipathic peptides.
摘要
研究人员采用取向样品固态 NMR 光谱法研究了两亲性抗菌肽鱼精肽 1 在磁场定向磷脂双层中的结构。在 25°C 至 61°C 之间进行的 (31)P NMR 和双共振 (1)H/(15)N NMR 实验能够在一系列温度下监测脂质头部基团和肽酰胺位点。该α-螺旋肽显著影响阴离子双层的相行为和结构，但不影响两性离子双层的相行为和结构。鱼精肽 1 稳定阴离子双层，当鱼精肽 1 位于膜表面时，这些双层在 61°C 下仍保持良好的取向。二维分离局部场实验表明，肽的倾斜角为 80±5°，与之前关于机械定向双层的结果一致。在这些条件下，肽在双层法向上快速旋转扩散，这些研究表明，磁场定向双层非常适合研究两亲肽。
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