| Autor: |
Hu, Kuan, Yin, Feng, Zhou, Ziyuan, Lian, Chenshan, Liu, Yinghuan, Sun, Chengjie, Li, Wenjun, Zhang, Jianing, Li, Zigang |
| Předmět: |
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| Zdroj: |
Chemical Communications; 9/11/2019, Vol. 55 Issue 70, p10484-10487, 4p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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