Cover Feature: Effect of Stapling Architecture on Physiochemical Properties and Cell Permeability of Stapled α‐Helical Peptides: A Comparative Study (ChemBioChem 21/2017),ChemBioChem

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Cover Feature: Effect of Stapling Architecture on Physiochemical Properties and Cell Permeability of Stapled α‐Helical Peptides: A Comparative Study (ChemBioChem 21/2017)
ChemBioChem ( IF 2.6 ) Pub Date : 2017-10-17 , DOI: 10.1002/cbic.201700551
Yuan Tian _{1,

2} , Yanhong Jiang ₁ , Jingxu Li ₁ , Dongyuan Wang ₁ , Hui Zhao ₁ , Zigang Li ₁

Affiliation

The cover feature shows a comparative study of the effect of different stapling architectures on the physiochemical properties and cell permeability of stapled peptides. The choice of stapling architecture exhibits the decisive impact of the properties of the crosslinkers on cell permeability, rather than peptides′ helical contents, in a model amphipathic sequence targeting the interaction between the estrogen receptor and its coactivator. This finding should shed further light on the chemical optimization of stapled α‐helical peptides or macrocyclic cell‐penetrating peptides for enhanced penetration. More information can be found in the communication by Z. Li et al. on page 2087 in Issue 21, 2017 (DOI: 10.1002/cbic.201700352).

中文翻译：

封面文章：钉合结构对钉合的α-螺旋肽的理化性质和细胞渗透性的影响：一项比较研究（ChemBioChem 21/2017）

覆盖特征显示了对不同缝合结构对钉合肽的理化性质和细胞通透性的影响的比较研究。在靶向雌激素受体与其共活化剂之间相互作用的模型两亲序列中，缝合结构的选择对细胞渗透性的决定性影响表现出决定性的影响，而不是肽的螺旋含量。该发现应进一步阐明钉合α-螺旋肽或大环细胞穿透肽的化学优化以增强渗透性。Z. Li等人在来文中可以找到更多信息。就在问题21，2017年2087页（：10.1002 / cbic.201700352 DOI）。

更新日期：2017-10-17

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