Histidine-Rich Cell-Penetrating Peptide for Cancer Drug Delivery and Its Uptake Mechanism

文献类型： 外文期刊

第一作者： Zhang, Lei

作者： Zhang, Lei;Ouyang, Pingkai;Chen, P.;Zhang, Lei;Xu, Jiang;Din, Yong;Wang, Toby;Martz, Matthew;Chen, P.;Zhang, Lei;Xu, Jiang;Wang, Fen;Din, Yong;Jin, Grace;Martz, Matthew;Chen, P.;Zhang, Lei;Gui, Zhongzheng;Zhang, Lei;Gui, Zhongzheng

作者机构：

期刊名称：LANGMUIR （ 影响因子：3.882； 五年影响因子：3.908 ）

ISSN： 0743-7463

年卷期： 2019 年 35 卷 9 期

页码：

收录情况： SCI

摘要： In this work, we report a drug delivery system based on the pH-responsive self-assembly and -disassembly behaviors of peptides. Here, a systematically designed histidine-rich lipidated peptide (NP1) is presented to encapsulate and deliver an anticancer drug ellipticine (EPT) into two model cells: non-small-cell lung carcinoma and Chinese hamster ovary cells. The mechanism of pH-responsive peptide self-assembly and -disassembly involved in the drug encapsulation and release process are extensively investigated. We found that NP1 could self-assemble as a spherical nanocomplex (diameter = 34.43 nm) in a neutral pH environment with EPT encapsulated and positively charged arginine amino acids aligned outward and EPT is released in an acidic environment due to the pH-triggered disassembly. Furthermore, the EPT-encapsulating peptide could achieve a mass loading ability of 18% (mass of loaded-EPT/mass of NP1) with optimization. More importantly, it is revealed that the positively charged arginine on the periphery of the NP1 peptides could greatly facilitate their direct translocation through the negatively charged plasma membrane via electrostatic interaction, instead of via endocytosis, which provides a more efficient uptake pathway.

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