Izumi Kayano, Saito Chihiro, Kawano Ryuji
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
Micromachines (Basel). 2023 Feb 2;14(2):373. doi: 10.3390/mi14020373.
This paper presents an investigation of liposome deformation and shape distortion using four membrane-binding peptides: TAT and C105Y as cell-penetrating peptides (CPPs), and melittin and ovispirin as antimicrobial peptides (AMPs). Liposome deformation was monitored utilizing fluorescent microscopy, while the binding of peptides to the DOPC membrane was estimated through capacitance measurements. The degree of liposome deformation and shape distortion was found to be higher for the CPPs compared to the AMPs. Additionally, it was observed that C105Y did not induce liposome rupture, unlike the other three peptides. We propose that these variations in liposome distortion may be attributed to differences in secondary structure, specifically the presence of an α-helix or random coil. Our studies offer insight into the use of peptides to elicit control of liposome architecture and may offer a promising approach for regulating the bodies of liposomal molecular robots.
作为细胞穿透肽（CPPs）的TAT和C105Y，以及作为抗菌肽（AMPs）的蜂毒肽和卵清蛋白。利用荧光显微镜监测脂质体变形，同时通过电容测量估计肽与二油酰磷脂酰胆碱（DOPC）膜的结合。结果发现，与抗菌肽相比，细胞穿透肽导致的脂质体变形和形状扭曲程度更高。此外，观察到与其他三种肽不同，C105Y不会诱导脂质体破裂。我们认为，脂质体扭曲的这些差异可能归因于二级结构的差异，特别是α-螺旋或无规卷曲的存在。我们的研究为利用肽来控制脂质体结构提供了见解，并可能为调节脂质体分子机器人的主体提供一种有前景的方法。
