A highly controllable protein self-assembly system with morphological versatility induced by reengineered host–guest interactions. Issue 23 (2nd June 2017)
- Record Type:
- Journal Article
- Title:
- A highly controllable protein self-assembly system with morphological versatility induced by reengineered host–guest interactions. Issue 23 (2nd June 2017)
- Main Title:
- A highly controllable protein self-assembly system with morphological versatility induced by reengineered host–guest interactions
- Authors:
- Li, Xiumei
Bai, Yushi
Huang, Zupeng
Si, Chengye
Dong, Zeyuan
Luo, Quan
Liu, Junqiu - Abstract:
- Abstract : A highly controllable protein self-assembly system with morphological diversity was constructed induced by a versatile site-specific protein modification tool. Abstract : Manipulating proteins to self-assemble into highly ordered nanostructures not only provides insights into the natural protein assembly process but also allows access to advanced biomaterials. Host–guest interactions have been widely used in the construction of artificial protein assemblies in recent years. CB[8] can selectively associate with two tripeptide Phe-Gly-Gly (FGG) tags with an extraordinarily high binding affinity ( K ter = 1.5 × 10 11 M −2 ). However, the FGG tags utilized before are all fixed to the N-termini via genetic fusion; this spatial limitation greatly confined the availability of the CB[8]/FGG pair in the construction of more sophisticated protein nanostructures. Here we first designed and synthesized a maleimide-functionalized Phe-Gly-Gly tag as a versatile site-specific protein modification tool; this designed tag can site-selectively introduce desired guest moieties onto protein surfaces for host–guest driven protein assembly. When regulating the self-assembly process of proteins and CB[8], the constructed protein nanosystem can exhibit distinctive morphological diversities ranging from nanorings, nanospirals, nanowires to superwires. This work developed a new strategy for site-specific protein modification of the CB[8] binding tag and provides a possible direction forAbstract : A highly controllable protein self-assembly system with morphological diversity was constructed induced by a versatile site-specific protein modification tool. Abstract : Manipulating proteins to self-assemble into highly ordered nanostructures not only provides insights into the natural protein assembly process but also allows access to advanced biomaterials. Host–guest interactions have been widely used in the construction of artificial protein assemblies in recent years. CB[8] can selectively associate with two tripeptide Phe-Gly-Gly (FGG) tags with an extraordinarily high binding affinity ( K ter = 1.5 × 10 11 M −2 ). However, the FGG tags utilized before are all fixed to the N-termini via genetic fusion; this spatial limitation greatly confined the availability of the CB[8]/FGG pair in the construction of more sophisticated protein nanostructures. Here we first designed and synthesized a maleimide-functionalized Phe-Gly-Gly tag as a versatile site-specific protein modification tool; this designed tag can site-selectively introduce desired guest moieties onto protein surfaces for host–guest driven protein assembly. When regulating the self-assembly process of proteins and CB[8], the constructed protein nanosystem can exhibit distinctive morphological diversities ranging from nanorings, nanospirals, nanowires to superwires. This work developed a new strategy for site-specific protein modification of the CB[8] binding tag and provides a possible direction for the construction of 'smart', dynamic self-assembly systems. … (more)
- Is Part Of:
- Nanoscale. Volume 9:Issue 23(2017)
- Journal:
- Nanoscale
- Issue:
- Volume 9:Issue 23(2017)
- Issue Display:
- Volume 9, Issue 23 (2017)
- Year:
- 2017
- Volume:
- 9
- Issue:
- 23
- Issue Sort Value:
- 2017-0009-0023-0000
- Page Start:
- 7991
- Page End:
- 7997
- Publication Date:
- 2017-06-02
- 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/c7nr01612c ↗
- 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:
- 185.xml