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Insight into the Mechanism of Internalization of the Cell-Penetrating Carrier Peptide Pep-1 by Conformational Analysis.
Journal of Biomedical Nanotechnology ( IF 2.9 ) Pub Date : 2020-12-15 , DOI: 10.1166/jbn.2020.2950
Ting Wang , Chu Wang , Size Zheng , Guanwen Qu , Zhangqi Feng , Jing Shang , Yaozhong Cheng , Nongyue He

Different secondary structures of the pep-1 protein were blamed for transmembrane internalization process of drugs and drug deliveries. But which structure will be important for transmembrane delivery was still not clear. In this study, interactions between pep-1 and cell membranes were studied. Pep-1 in the buffer (Pep-1) and pep-1 on graphene (PDS/G) or they on graphene oxide (PDS/GO) were composed as the transmembrane delivery system to study the different secondary structure of pep-1 that influence for their transmembrane delivery. The curves of chirascan circular dichroism (CD) and all-atom discontinuous molecular dynamics (DMD) simulations illuminate that, in a buffer environment, most pep-1 formed 3-10 helix structures. Meanwhile, when Pep-1 composed graphene slice and formed PDS/G, 3-10 helix and alpha-helix structures can be found in small quantities. When they on graphene oxide and formed PDS/GO, coil or type II beta-turn structure can be found from most of the pep-1 and 3-10 helix structure disappeared. By using sum-frequency generation (SFG) vibrational spectroscopy, we found that pep-1 with 3-10 helix structures in buffer solutions damaged the lipid bilayer violently. PDS/G with less 3-10 helix structures will change the orientation of lipid bilayer effectively but slightly. Pep-1 with coil or type II Beta-turn in PDS/GO cannot influence the structure of lipid bilayers. Hemolysis experiments also proved that when pep-1 composed as PDS/G, they will change the orientation of the plasma membrane of red blood cells effectively but slightly. When they attach on the GO and formed PDS/GO, the plasma membrane of red blood cells cannot be influenced. In conclusion, 3-10 helix structures will be positively correlated with disturbance of membranes. These results will be effectively guided the clinic application of pep-1 as a transporter of the drug delivery system.

中文翻译:

通过构象分析洞察细胞穿透载体肽Pep-1的内在化机理。

pep-1蛋白的不同二级结构被归因于药物的跨膜内在化过程和药物递送。但是哪种结构对于跨膜递送将是重要的仍不清楚。在这项研究中,pep-1和细胞膜之间的相互作用进行了研究。缓冲液中的Pep-1(Pep-1)和石墨烯上的pep-1(PDS / G)或氧化石墨烯上的pep-1(PDS / GO)组成跨膜递送系统,研究pep-1的不同二级结构跨膜输送的影响。chirascan圆二色性(CD)和全原子不连续分子动力学(DMD)模拟的曲线说明,在缓冲环境中,大多数pep-1形成3-10螺旋结构。同时,当Pep-1组成石墨烯切片并形成PDS / G时,可以发现少量的3-10螺旋和α-螺旋结构。当它们在氧化石墨烯上形成PDS / GO时,可以从大多数pep-1中发现线圈或II型β转角结构,而3-10螺旋结构消失了。通过使用和频生成(SFG)振动光谱,我们发现在缓冲溶液中具有3-10螺旋结构的pep-1强烈破坏了脂质双层。具有较少3-10螺旋结构的PDS / G将有效但略微改变脂质双层的方向。Pes-1在PDS / GO中带有线圈或II型β转角不能影响脂质双层的结构。溶血实验还证明,当pep-1组成PDS / G时,它们可以有效但略微改变红细胞质膜的方向。当他们附着在GO上并形成PDS / GO时,红细胞的质膜不会受到影响。总之,3-10螺旋结构将与膜的扰动正相关。这些结果将有效指导pep-1作为药物输送系统转运蛋白的临床应用。
更新日期:2020-12-16
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