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Directional assembly of a stapled α-helical peptide

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Abstract

The de novo design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX)2-NH2, transformed from a random coil to an α-helical structure upon disulphide bonding of the flanking cysteine residues positioning at the i/i + 4 locations. The stapling form of this peptide enforces a conformational restraint that affords the driving force for self-assembly into nanorod/nanovesicle structures. Moreover, these assembled materials can transport siRNA into cancer cells and immediately release the cargo in a reductive environment.

Graphical abstract: Directional assembly of a stapled α-helical peptide

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Publication details

The article was received on 16 Jun 2019, accepted on 05 Aug 2019 and first published on 05 Aug 2019


Article type: Communication
DOI: 10.1039/C9CC04591K
Chem. Commun., 2019, Advance Article

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    Directional assembly of a stapled α-helical peptide

    K. Hu, F. Yin, Z. Zhou, C. Lian, Y. Liu, C. Sun, W. Li, J. Zhang and Z. Li, Chem. Commun., 2019, Advance Article , DOI: 10.1039/C9CC04591K

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