Achieving enhanced cell penetration of short conformationally constrained peptides through amphiphilicity tuning

Yuan Tian, Xiangze Zeng, Jingxu Li, Yanhong Jiang, Hui Zhao, Dongyuan Wang, Xuhui Huang*, Zigang Li*

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

32 Citations (Scopus)

Abstract

Due to their enhanced stability and cell permeability, cyclic cell-penetrating peptides have been widely used as delivery vectors for transporting cell-impermeable cargos into cells. In this study, we synthesized a panel of conformationally constrained peptides with either α-helix or β-hairpin conformations. We tuned the amphiphilicity of these constrained peptides with different distributions of charged or hydrophobic residues and compared their cellular uptake efficiencies in different cell lines. We found that the amphipathicity of these conformationally constrained peptides correlates well with their cellular uptake efficiency. We proposed that peptides with larger hydrophobic moments (HMs) have stronger binding affinities with the cell membrane which further accelerates the endocytosis process. This finding should provide an approach towards the design of more potent conformationally constrained cell-penetrating peptides for biomedical applications.

Original languageEnglish
Pages (from-to)7576-7581
Number of pages6
JournalChemical Science
Volume8
Issue number11
DOIs
Publication statusPublished - 1 Nov 2017

Scopus Subject Areas

  • Chemistry(all)

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