Achieving higher hierarchical structures by cooperative assembly of tripeptides with reverse sequences. Issue 16 (5th April 2023)
- Record Type:
- Journal Article
- Title:
- Achieving higher hierarchical structures by cooperative assembly of tripeptides with reverse sequences. Issue 16 (5th April 2023)
- Main Title:
- Achieving higher hierarchical structures by cooperative assembly of tripeptides with reverse sequences
- Authors:
- Wang, Zhongyan
Shang, Yuna
Luo, Hongjing
Yang, Cuihong
Yang, Zhimou
Ren, Chunhua
Liu, Jianfeng - Abstract:
- Abstract : We report a novel strategy for achieving low-to-high hierarchical structure transformation through the cooperative self-assembly of naphthyl-capped tripeptides with reverse sequences. Abstract : Hierarchical self-assembly based on peptides in nature is a multi-component interaction process, providing a broad platform for various bionanotechnological applications. However, the study of controlling the hierarchical structure transformation via the cooperation rules of different sequences is still rarely reported. Herein, we report a novel strategy of achieving higher hierarchical structures through cooperative self-assembly of hydrophobic tripeptides with reverse sequences. We unexpectedly found that Nap-FVY and its reverse sequence Nap-YVF self-assembled into nanospheres, respectively, while their mixture formed nanofibers, obviously exhibiting a low-to-high hierarchical structure transformation. Further, this phenomenon was demonstrated by the other two collocations. The cooperation of Nap-VYF and Nap-FYV afforded the transformation from nanofibers to twisted nanoribbons, and the cooperation of Nap-VFY and Nap-YFV realized the transformation from nanoribbons to nanotubes. The reason may be that the cooperative systems in the anti-parallel β-sheet conformation created more hydrogen bond interactions and in-register π–π stacking, promoting a more compact molecular arrangement. This work provides a handy approach for controlled hierarchical assembly and theAbstract : We report a novel strategy for achieving low-to-high hierarchical structure transformation through the cooperative self-assembly of naphthyl-capped tripeptides with reverse sequences. Abstract : Hierarchical self-assembly based on peptides in nature is a multi-component interaction process, providing a broad platform for various bionanotechnological applications. However, the study of controlling the hierarchical structure transformation via the cooperation rules of different sequences is still rarely reported. Herein, we report a novel strategy of achieving higher hierarchical structures through cooperative self-assembly of hydrophobic tripeptides with reverse sequences. We unexpectedly found that Nap-FVY and its reverse sequence Nap-YVF self-assembled into nanospheres, respectively, while their mixture formed nanofibers, obviously exhibiting a low-to-high hierarchical structure transformation. Further, this phenomenon was demonstrated by the other two collocations. The cooperation of Nap-VYF and Nap-FYV afforded the transformation from nanofibers to twisted nanoribbons, and the cooperation of Nap-VFY and Nap-YFV realized the transformation from nanoribbons to nanotubes. The reason may be that the cooperative systems in the anti-parallel β-sheet conformation created more hydrogen bond interactions and in-register π–π stacking, promoting a more compact molecular arrangement. This work provides a handy approach for controlled hierarchical assembly and the development of various functional bionanomaterials. … (more)
- Is Part Of:
- Nanoscale. Volume 15:Issue 16(2023)
- Journal:
- Nanoscale
- Issue:
- Volume 15:Issue 16(2023)
- Issue Display:
- Volume 15, Issue 16 (2023)
- Year:
- 2023
- Volume:
- 15
- Issue:
- 16
- Issue Sort Value:
- 2023-0015-0016-0000
- Page Start:
- 7502
- Page End:
- 7509
- Publication Date:
- 2023-04-05
- Subjects:
- Nanoscience -- Periodicals
Nanotechnology -- Periodicals
620.505 - Journal URLs:
- http://www.rsc.org/Publishing/Journals/NR/Index.asp ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d3nr00983a ↗
- Languages:
- English
- ISSNs:
- 2040-3364
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9830.266000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 27036.xml