Directional assembly of a stapled α-helical peptide
Chemical Communications2019Vol. 55(70), pp. 10484–10487
Citations Over Time
Kuan Hu, Feng Yin, Ziyuan Zhou, Chenshan Lian, Yinghuan Liu, Chengjie Sun, Wenjun Li, Jianing Zhang, Zigang Li
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.
Related Papers
- Susquehanna Chorale Spring Concert "Roots and Wings"(2017)
- → DETERMINING QUALITY REQUIREMENTS AT THE UNIVERSITIES TO IMPROVE THE QUALITY OF EDUCATION(2018)
- Коммуникaтивно- прaгмaтический aнaлиз дипломaтических бумaг (нa основе вербaльных нот)(2018)
- → ФОРМИРОВAНИЕ ГОТОВНОСТИ БУДУЩИХ ПЕДAГОГОВ К ОРГAНИЗAЦИИ РAБОТЫ ПО РAЗВИТИЮ ВAЛЕОЛОГИЧЕСКОЙ КУЛЬТУРЫ ШКОЛЬНИКОВ(2023)