Assessing topology and surface orientation of an antimicrobial peptide magainin 2 using mechanically aligned bilayers and electron paramagnetic resonance spectroscopy
Assessing topology and surface orientation of an antimicrobial peptide magainin 2 using mechanically aligned bilayers and electron paramagnetic resonance spectroscopy
复制标题
DOI：
10.1016/j.chemphyslip.2018.04.004
复制
发表时间：
2018-07-01
影响因子：
3.4
通讯作者：
Lorigan, Gary A.
中科院分区：
文献类型：
--
作者：
Mayo, Daniel J.;Sahu, Indra D.;Lorigan, Gary A.
排列的CW-EPR膜蛋白样品提供了传统随机分散样品所没有的额外的拓扑相互作用。这些样品非常适合研究抗菌肽，因为它们的动态外围拓扑结构。本研究合成了4个连续取代的抗菌肽模型magainin 2，并用刚性TOAC自旋标记进行了标记。结果表明，TOAC取代H7、S8、A9和K10的螺旋倾角分别为66°+/- 5°、76°+/- 5°、70°+/- 5°和72°+/- 5°。这些结果与先前发表的文献一致。利用电子顺磁共振（EPR）机械定位技术，这些取代被用来严格评估肽相对于膜的拓扑结构和表面取向。这种方法提供了一种快速和简单的方法来研究抗菌肽的结构拓扑。
Aligned CW-EPR membrane protein samples provide additional topology interactions that are absent from conventional randomly dispersed samples. These samples are aptly suited to studying antimicrobial peptides because of their dynamic peripheral topology. In this study, four consecutive substitutions of the model antimicrobial peptide magainin 2 were synthesized and labeled with the rigid TOAC spin label. The results revealed the helical tilts to be 66 degrees +/- 5 degrees, 76 degrees +/- 5 degrees, 70 degrees +/- 5 degrees, and 72 degrees +/- 5 degrees for the TOAC substitutions H7, S8, A9, and K10 respectively. These results are consistent with previously published literature. Using the EPR (electron paramagnetic resonance) mechanical alignment technique, these substitutions were used to critically assess the topology and surface orientation of the peptide with respect to the membrane. This methodology offers a rapid and simple approach to investigate the structural topology of antimicrobial peptides.