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° ± 5°, 76° ± 5°, 70° ± 5°, and 72° ± 5° 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.

对齐的CW-EPR膜蛋白样品提供了常规随机分散样品所没有的其他拓扑相互作用。这些样品因其动态外围拓扑结构而非常适合研究抗菌肽。在这项研究中，模型抗菌肽magainin 2的四个连续取代被合成并用刚性TOAC自旋标记物标记。结果表明，TOAC替代品H7，S8，A9和K10的螺旋倾斜度分别为66°±5°，76°±5°，70°±5°和72°±5°。这些结果与先前发表的文献一致。使用EPR（电子顺磁共振）机械比对技术，这些取代可用于严格评估肽相对于膜的拓扑和表面取向。