Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
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DOI：
10.1016/j.bbamem.2010.03.005
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发表时间：
2010-06-01
影响因子：
3.4
通讯作者：
Deshayes, Sebastien
中科院分区：
文献类型：
--
作者：
Eiriksdottir, Emelia;Konate, Karidia;Deshayes, Sebastien
由于生物膜的渗透性差，临床上有效治疗药物的使用常常受到限制。为了增强两亲性短肽的细胞传递能力，细胞穿透肽（CPPs）在过去的二十年中得到了广泛的研究。CPPs基于蛋白质转导结构域、模型肽或嵌合结构，并已被用于通过共价或非共价策略将货物输送到细胞中。尽管多个参数同时参与其内化机制，但最近对CPPs的关注表明，CPPs的结构特性及其与膜磷脂的相互作用可能在细胞摄取机制中发挥重要作用。在目前的工作中，我们报告了10种已知的CPPs的结构可塑性及其与磷脂膜相互作用的能力的比较分析。我们根据文献中报道的CPPs的结构特性、对磷脂的亲和力和内化途径提出了一种新的分类方法。(C) 2010 Elsevier B.V.版权所有
The clinical use of efficient therapeutic agents is often limited by the poor permeability of the biological membranes. In order to enhance their cell delivery, short amphipathic peptides called cell-penetrating peptides (CPPs) have been intensively developed for the last two decades. CPPs are based either on protein transduction domains, model peptide or chimeric constructs and have been used to deliver cargoes into cells through either covalent or non-covalent strategies. Although several parameters are simultaneously involved in their internalization mechanism, recent focuses on CPPs suggested that structural properties and interactions with membrane phospholipids could play a major role in the cellular uptake mechanism. In the present work, we report a comparative analysis of the structural plasticity of 10 well-known CPPs as well as their ability to interact with phospholipid membranes. We propose a new classification of CPPs based on their structural properties, affinity for phospholipids and internalization pathways already reported in the literature. (C) 2010 Elsevier B.V. All rights reserved.