The LAH4 family of amphipathic peptides exhibits pronounced antimicrobial, cell penetrating and nucleic acid transfection activities. Furthermore, variants were designed with potent lentiviral transduction enhancement. When viewed along a helical wheel the four histidines are arranged to form an amphipathic structure. In order to optimize some of these biological activities the number of leucine and alanine residues exposed to the hydrophilic surface was systematically varied which resulted in the design of vectofusin a peptide with strong lentiviral transduction enhancement activities. Here the series of peptides with varying numbers of alanine or leucine residues, respectively, framed by the histidines was tested for their calcein release activity. Interestingly, the membrane pore formation and DNA transfection activities show a clear correlation with the hydrophilic angle. In contrast the membrane partitioning and the propensity to adopt helical conformations was hardly affected as long as the hydrophilic angle did not exceed a limiting value of 150°.

中文翻译：

---

膜孔的形成与具有多种生物学活性的富含组氨酸的两亲性肽的亲水角相关。

LAH4两亲性肽家族表现出显着的抗微生物，细胞穿透和核酸转染活性。此外，设计了具有有效慢病毒转导增强功能的变体。当沿螺旋轮观察时，四个组氨酸排列成两亲结构。为了优化这些生物活性中的一些，系统地改变暴露于亲水表面的亮氨酸和丙氨酸残基的数量，这导致设计了具有强大的慢病毒转导增强活性的vecofusinin肽。在此，测试了由组氨酸分别构图的具有不同数量的丙氨酸或亮氨酸残基的一系列肽的钙黄绿素释放活性。有趣的是 膜孔的形成和DNA转染活性与亲水角呈明显的相关性。相反，只要亲水角不超过150°的极限值，几乎不影响膜的分隔和采用螺旋构象的倾向。