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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)
Author(s) -
Tian Yuan,
Jiang Yanhong,
Li Jingxu,
Wang Dongyuan,
Zhao Hui,
Li Zigang
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700551
Subject(s) - amphiphile , cell permeability , chemistry , penetration (warfare) , cell penetrating peptide , peptide , biophysics , cell , combinatorial chemistry , cover (algebra) , permeability (electromagnetism) , stereochemistry , biochemistry , computational biology , copolymer , biology , organic chemistry , engineering , mechanical engineering , membrane , operations research , polymer
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).