Structural polymorphism of two CPP: An important parameter of activity
Structural polymorphism of two CPP: An important parameter of activity
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DOI：
10.1016/j.bbamem.2008.01.027
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发表时间：
2008-05-01
影响因子：
3.4
通讯作者：
Thomas, Annick
中科院分区：
文献类型：
--
作者：
Deshayes, Sebastien;Decaffmeyer, Marc;Thomas, Annick
尽管进行了大量的研究，但细胞穿透肽（CPP）的重要结构特征仍然不清楚，这一点在设计新分子时遇到了困难。在这项研究中，我们将我们的兴趣集中在Penetratin和Transportan及其几个变体上。Penetratin W 48 F和Penetratin W 48 F/W56 F分别表现出细胞摄取减少和完全缺乏; TP 07和TP 10表现出与Transportan相似的细胞摄取，TP 08、TP 13和TP 15表现出无内化能力或内化能力较弱。我们应用PepLook算法分析多肽多态性。该研究揭示了CPP及其可渗透变体的共同构象特征：它们都是多态性的。阴性、非渗透性突变体具有相反的特征，因为它们是单态的。最后，我们支持的假设，结构多态性可能是至关重要的，因为它提供了肽的可能性，以适应他们的构象介质的疏水性和/或合作伙伴的多样性。(C)2008 Elsevier B. V.保留所有权利。
Despite numerous investigations, the important structural features of Cell Penetrating Peptides (CPPs) remain unclear as demonstrated by the difficulties encountered in designing new molecules. In this study, we focused our interest on Penetratin and Transportan and several of their variants. Penetratin W48F and Penetratin W48F/W56F exhibit a reduced and a complete lack of cellular uptake, respectively; TP07 and TP10 present a similar cellular uptake as Transportan and TP08, TP13 and TP15 display no or weak internalization capacity. We applied the algorithmic method named PepLook to analyze the peptide polymorphism. The study reveals common conformational characteristics for the CPPs and their permeable variants: they all are polymorphic. Negative, non permeable, mutants share the opposite feature since they are monomorphic. Finally, we support the hypothesis that structural polymorphism may be crucial since it provides peptides with the possibility of adapting their conformation to medium hydrophobicity and or to partner diversity. (C) 2008 Elsevier B.V. All rights reserved.