Group 3 LEA protein model peptides protect liposomes during desiccation
Group 3 LEA protein model peptides protect liposomes during desiccation
复制标题
DOI：
10.1016/j.bbamem.2014.07.009
复制
发表时间：
2014-11-01
影响因子：
3.4
通讯作者：
Sakurai, Minoru
中科院分区：
文献类型：
--
作者：
Furuki, Takao;Sakurai, Minoru
我们研究了我们在以前的研究中开发的第3组莱亚（G3莱亚）蛋白的模型肽是否可以保护脂质体免受干燥损伤。比较了四种不同的肽：1）Pv莱亚-22，其由来自非洲睡眠摇蚊的莱亚蛋白的特征性11-mer基序的两个串联重复组成; 2）氨基酸组成与Pv莱亚-22相同但其序列乱序的肽; 3）聚-L-谷氨酸;和4）聚-L-赖氨酸。肽1）和2）保护由1-棕榈酰基2-油酰基-sn-甘油基-3-磷脂酰胆碱（POPC）组成的脂质体免受由干燥引起的融合，如通过动态光散射的粒度分布测量所揭示的。实际上，当以大于0.5的肽/POPC摩尔比添加这些肽时，脂质体保持其预应力尺寸分布。有趣的是，肽1）实现了与先前公开的几种天然莱亚蛋白质相当或更高的荧光探针在脂质体内的保留。相比之下，其他肽表现出较少的保护作用。这些结果表明，源自G3 LEA蛋白序列的合成肽可以抑制干燥诱导的脂质体融合。对每种肽和脂质体的干燥混合物进行傅里叶变换红外（FT-IR）光谱测量。基于脂质体的凝胶-液晶相变温度和肽骨架的二级结构的结果，我们讨论了合成肽对干燥脂质体的保护作用的可能的潜在机制。(C)2014爱思唯尔有限公司版权所有。
We investigated whether a model peptide for group 3 LEA (G3LEA) proteins we developed in previous studies can protect liposomes from desiccation damage. Four different peptides were compared: 1) PvLEA-22, which consists of two tandem repeats of the 11-mer motif characteristic of LEA proteins from the African sleeping chironomid; 2) a peptide with amino acid composition identical to that of PvLEA-22, but with its sequence scrambled; 3) poly-L-glutamic acid; and 4) poly-L-lysine. Peptides 1) and 2) protected liposomes composed of 1-palmitoyl 2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) against fusion caused by desiccation, as revealed by particle size distribution measurements with dynamic light scattering. Indeed, liposomes maintain their pre-stress size distribution when these peptides are added at a peptide/POPC molar ratio of more than 0.5. Interestingly, peptide 1) achieved the comparable or higher retention of a fluorescent probe inside liposomes than did several native LEA proteins published previously. In contrast, the other peptides exhibited less protective effects. These results demonstrate that the synthetic peptide derived from the G3LEA protein sequence can suppress desiccation-induced liposome fusion. Fourier transform infrared (FT-IR) spectroscopic measurements were performed for the dried mixture of each peptide and liposome. Based on results for the gel-to-liquid crystalline phase transition temperature of the liposome and the secondary structure of the peptide backbone, we discuss possible underlying mechanisms for the protection effect of the synthetic peptide on dried liposomes. (C) 2014 Elsevier B.V. All rights reserved.