Directional assembly of a stapled α-helical peptide

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 -NH 2 , transformed from a random...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2019-08, Vol.55 (7), p.1484-1487
Main Authors: Hu, Kuan, Yin, Feng, Zhou, Ziyuan, Lian, Chenshan, Liu, Yinghuan, Sun, Chengjie, Li, Wenjun, Zhang, Jianing, Li, Zigang
Format: Article
Language:English
Subjects:
Assembling
Coils
Microscopy, Atomic Force
Nanorods
Oxidation
Oxidation-Reduction
Peptides
Peptides - chemistry
Protein Conformation, alpha-Helical
Self-assembly
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Summary: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 -NH 2 , 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. In this work, we described a method to control the helical peptide self-assembly by stapling the peptide via an intramolecular disulfide bridge.
ISSN:1359-7345
1364-548X
DOI:10.1039/c9cc04591k