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Issue 70, 2019
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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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Article information


Submitted
16 Jun 2019
Accepted
05 Aug 2019
First published
05 Aug 2019

Chem. Commun., 2019,55, 10484-10487
Article type
Communication

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, 55, 10484
DOI: 10.1039/C9CC04591K

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