Journal
CHEMICAL COMMUNICATIONS
Volume 55, Issue 70, Pages 10484-10487Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc04591k
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Funding
- Natural Science Foundation of China [21778009, 81701818, 21801019]
- Shenzhen Science and Technology Innovation Committee [JCYJ20170412150719814, GJHS20170310093122365]
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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 alpha-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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