Construction of a smart temperature-responsive GPx mimic based on the self-assembly of supra-amphiphiles. Issue 4 (30th November 2015)
- Record Type:
- Journal Article
- Title:
- Construction of a smart temperature-responsive GPx mimic based on the self-assembly of supra-amphiphiles. Issue 4 (30th November 2015)
- Main Title:
- Construction of a smart temperature-responsive GPx mimic based on the self-assembly of supra-amphiphiles
- Authors:
- Zou, Huixin
Sun, Hongcheng
Wang, Liang
Zhao, Linlu
Li, Jiaxi
Dong, Zeyuan
Luo, Quan
Xu, Jiayun
Liu, Junqiu - Abstract:
- Abstract : A supra-amphiphilic thermosensitive vesicle-like structure was designed by the self-assembly of host–guest interaction to construct a smart artificial GPx mimic with controllable catalytic activity. Abstract : Glutathione peroxidase (GPx) is a major defense against hydroperoxides as a kind of seleno-enzyme that protects cells from oxidative damage. A supramolecular vesicle with controllable GPx activity and morphology has been successfully constructed by the self-assembly of supra-amphiphiles formed by host–guest recognition between cyclodextrin and adamantane derivatives. By introducing thermosensitive poly( N -isopropylacrylamide) (PNIPAM) scaffolds and the catalytic moiety selenium into adamantane and cyclodextrin, respectively, the complex of catalysis-functionalized cyclodextrin with thermosensitivity-functionalized adamantane directed the formation of a supramolecular vesicle which acted as a GPx mimic at 37 °C. The self-assembled nanoenzyme exhibited an obvious temperature responsive characteristic and high GPx-like catalytic activity promoting the reduction of hydrogen peroxide (H2 O2 ) with glutathione (GSH) as the reducing substrate at 37 °C. However, the vesicle disassembled when the temperature decreased to 25 °C due to the transition of PNIPAM between the coil and the globule. Interestingly, the catalytic activity changed along with the transformation of morphologies. The vesicle structure self-assembled at 37 °C provided the favorableAbstract : A supra-amphiphilic thermosensitive vesicle-like structure was designed by the self-assembly of host–guest interaction to construct a smart artificial GPx mimic with controllable catalytic activity. Abstract : Glutathione peroxidase (GPx) is a major defense against hydroperoxides as a kind of seleno-enzyme that protects cells from oxidative damage. A supramolecular vesicle with controllable GPx activity and morphology has been successfully constructed by the self-assembly of supra-amphiphiles formed by host–guest recognition between cyclodextrin and adamantane derivatives. By introducing thermosensitive poly( N -isopropylacrylamide) (PNIPAM) scaffolds and the catalytic moiety selenium into adamantane and cyclodextrin, respectively, the complex of catalysis-functionalized cyclodextrin with thermosensitivity-functionalized adamantane directed the formation of a supramolecular vesicle which acted as a GPx mimic at 37 °C. The self-assembled nanoenzyme exhibited an obvious temperature responsive characteristic and high GPx-like catalytic activity promoting the reduction of hydrogen peroxide (H2 O2 ) with glutathione (GSH) as the reducing substrate at 37 °C. However, the vesicle disassembled when the temperature decreased to 25 °C due to the transition of PNIPAM between the coil and the globule. Interestingly, the catalytic activity changed along with the transformation of morphologies. The vesicle structure self-assembled at 37 °C provided the favorable microenvironment for the enzymatic reaction, hence we successfully developed a temperature-responsive nanoenzyme model. Moreover, the catalytic activity of the thermosensitive GPx mimic exhibited excellent reversibility and typical saturation kinetics behaviour similar to a natural enzyme catalyst. It is assumed that the proposed GPx model not only has remarkable advantages such as easy functionalization and facile preparation but also provided a new way to develop intelligent responsive materials. … (more)
- Is Part Of:
- Soft matter. Volume 12:Issue 4(2016)
- Journal:
- Soft matter
- Issue:
- Volume 12:Issue 4(2016)
- Issue Display:
- Volume 12, Issue 4 (2016)
- Year:
- 2016
- Volume:
- 12
- Issue:
- 4
- Issue Sort Value:
- 2016-0012-0004-0000
- Page Start:
- 1192
- Page End:
- 1199
- Publication Date:
- 2015-11-30
- Subjects:
- Soft condensed matter -- Periodicals
530.413 - Journal URLs:
- http://www.rsc.org/Publishing/Journals/sm/index.asp ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c5sm02074c ↗
- Languages:
- English
- ISSNs:
- 1744-683X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8321.419000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1295.xml