Directional assembly of a stapled α-helical peptide

Kuan Hu; Feng Yin; Ziyuan Zhou; Chenshan Lian; Yinghuan Liu; Chengjie Sun; Wenjun Li; Jianing Zhang; Zigang Li

doi:10.1039/c9cc04591k

Directional assembly of a stapled α-helical peptide

Kuan Hu, Feng Yin, Ziyuan Zhou, Chenshan Lian, Yinghuan Liu, Chengjie Sun, Wenjun Li, Jianing Zhang, Zigang Li^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

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.

Original language	English
Pages (from-to)	10484-10487
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	70
DOIs	https://doi.org/10.1039/c9cc04591k
Publication status	Published - 2019
Externally published	Yes

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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.",

author = "Kuan Hu and Feng Yin and Ziyuan Zhou and Chenshan Lian and Yinghuan Liu and Chengjie Sun and Wenjun Li and Jianing Zhang and Zigang Li",

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T1 - Directional assembly of a stapled α-helical peptide

AU - Hu, Kuan

AU - Yin, Feng

AU - Zhou, Ziyuan

AU - Lian, Chenshan

AU - Liu, Yinghuan

AU - Sun, Chengjie

AU - Li, Wenjun

AU - Zhang, Jianing

AU - Li, Zigang

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

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DO - 10.1039/c9cc04591k

M3 - Article

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AN - SCOPUS:85071670108

SN - 1359-7345

VL - 55

SP - 10484

EP - 10487

JO - Chemical Communications

JF - Chemical Communications

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ER -

Directional assembly of a stapled α-helical peptide

Abstract

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