The kinetic mechanism of cations induced protein nanotubes self-assembly and their application as delivery system. (July 2022)
- Record Type:
- Journal Article
- Title:
- The kinetic mechanism of cations induced protein nanotubes self-assembly and their application as delivery system. (July 2022)
- Main Title:
- The kinetic mechanism of cations induced protein nanotubes self-assembly and their application as delivery system
- Authors:
- Zhang, Jipeng
Wang, Qimeng
Liu, Bin
Li, Dan
Zhang, Huijuan
Wang, Pengjie
Liu, Jinfang
Hou, Guohua
Li, Xin
Yuan, Yu
Li, Zekun
Chen, Shanan
Yan, Huiling
Li, Yuan - Abstract:
- Abstract: The amphiphilic proteins can be used as building blocks (BBs) forming various self-assemblies. Understanding their self-assembly mechanism is important for designing novel nanomaterials. Herein, the BBs dimers were first prepared from carboxyl-abundant enzymolyzed α-lactalbumin (α-lac) at 50 °C. Then the unidentate coordination of Ca 2+ between the BBs caused a β-sheet stacking to further self-assemble into nanotubes (NTs). Compared with the traditional "one-pot" method, a step-wise new method was applied to study hydrolysis, aggregation and self-assembly processes separately. The α-lac was hydrolyzed into 11 kDa amphiphilic peptides independent of temperature while a BBs dimer was formed at 50 °C by hydrophobic interaction. Ca 2+ induced a conformational change of BBs and promoted these BBs gradually aggregate into 10 strands of filaments, which twisted into helical ribbons by electrostatic repulsion. Ca 2+ further induced the twisted helical ribbons closed into NTs driven by the reduction of line tension energy. Besides, the carboxyl-Ca 2+ coordination dominated NTs elongation in the longitudinal direction and filaments aggregation in the lateral direction with the same binding stoichiometry of 1:1 respectively. Finally, NTs successfully encapsulated curcumin and improved the viscosity of liquid food. α-Lac NTs show a high potential as a delivery system for food applications.
- Is Part Of:
- Biomaterials. Volume 286(2022)
- Journal:
- Biomaterials
- Issue:
- Volume 286(2022)
- Issue Display:
- Volume 286, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 286
- Issue:
- 2022
- Issue Sort Value:
- 2022-0286-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-07
- Subjects:
- Self-assembly -- Nanotubes -- Helical structures -- Calcium coordination -- α-Lactalbumin
Biomedical materials -- Periodicals
Biocompatible Materials -- Periodicals
Biomatériaux -- Périodiques
610.28 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01429612 ↗
http://www.clinicalkey.com/dura/browse/journalIssue/01429612 ↗
http://www.clinicalkey.com.au/dura/browse/journalIssue/01429612 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.biomaterials.2022.121600 ↗
- Languages:
- English
- ISSNs:
- 0142-9612
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2087.715000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21788.xml