Selective removal of IgG from the urine of patients with proteinuria using a polymer coated core–shell magnetic nanoparticle. Issue 109 (11th November 2016)
- Record Type:
- Journal Article
- Title:
- Selective removal of IgG from the urine of patients with proteinuria using a polymer coated core–shell magnetic nanoparticle. Issue 109 (11th November 2016)
- Main Title:
- Selective removal of IgG from the urine of patients with proteinuria using a polymer coated core–shell magnetic nanoparticle
- Authors:
- Deng, Zhifen
Hu, Kai
Bi, Liangliang
Yuan, Hang
Chen, Yanlong
Zhao, Shengnan
Du, Huifang
Yuan, Xuesheng
Huang, Yanjie
Zhang, Shusheng - Abstract:
- Abstract : A synthetic monomer of N -methacryloyl-l -aspartic acid plays a specific recognition role in magnetic separation of IgG from urinary protein sample using Fe3 O4 @SiO2 @MAsp-HEMA nanoparticles. Abstract : Selective removal of highly abundant proteins prior to analysis is an important issue in proteomics. In this study, a core–shell structured magnetic nanocomposite of Fe3 O4 @SiO2 @MAsp-HEMA was found to be an effective and selective adsorbent to remove highly abundant IgG from the urine of patients with proteinuria. This novel magnetic adsorbent was prepared by coating a poly( N -methacryloyl-l -aspartic acid-hydroxyethyl methacrylate) shell on Fe3 O4 @SiO2 nanoparticles via a coupling agent of KH-570 using the mini-emulsion polymerization method. The as-synthesized nanoparticle was characterized by X-ray diffraction, elemental analysis, thermal gravimetric analysis, infrared spectroscopy, magnetic hysteresis loop curves, scanning electronic microscopy and transmission electron microscopy. A kinetic adsorption experiment was performed to investigate the speed of adsorption and the time to reach the adsorption balance. 1D SDS-PAGE analysis and capillary electrophoresis were used to validate its selective adsorption ability. The resulting Fe3 O4 @SiO2 @MAsp-HEMA showed a uniform spherical shape at nanoscale dimensions of about 200–300 nm, removing efficiency above 80%, and maximum adsorption capacity of 18.08 μg mg −1 at 15 ± 0.5 °C. The binding between IgG and theAbstract : A synthetic monomer of N -methacryloyl-l -aspartic acid plays a specific recognition role in magnetic separation of IgG from urinary protein sample using Fe3 O4 @SiO2 @MAsp-HEMA nanoparticles. Abstract : Selective removal of highly abundant proteins prior to analysis is an important issue in proteomics. In this study, a core–shell structured magnetic nanocomposite of Fe3 O4 @SiO2 @MAsp-HEMA was found to be an effective and selective adsorbent to remove highly abundant IgG from the urine of patients with proteinuria. This novel magnetic adsorbent was prepared by coating a poly( N -methacryloyl-l -aspartic acid-hydroxyethyl methacrylate) shell on Fe3 O4 @SiO2 nanoparticles via a coupling agent of KH-570 using the mini-emulsion polymerization method. The as-synthesized nanoparticle was characterized by X-ray diffraction, elemental analysis, thermal gravimetric analysis, infrared spectroscopy, magnetic hysteresis loop curves, scanning electronic microscopy and transmission electron microscopy. A kinetic adsorption experiment was performed to investigate the speed of adsorption and the time to reach the adsorption balance. 1D SDS-PAGE analysis and capillary electrophoresis were used to validate its selective adsorption ability. The resulting Fe3 O4 @SiO2 @MAsp-HEMA showed a uniform spherical shape at nanoscale dimensions of about 200–300 nm, removing efficiency above 80%, and maximum adsorption capacity of 18.08 μg mg −1 at 15 ± 0.5 °C. The binding between IgG and the ligand was confirmed by isothermal titration calorimetry. The hydrogen bonding force was demonstrated as one of the major interactions between the functional groups of the as-synthesized magnetic nanoparticles and IgG by a molecular docking experiment. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 109(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 109(2016)
- Issue Display:
- Volume 6, Issue 109 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 109
- Issue Sort Value:
- 2016-0006-0109-0000
- Page Start:
- 107732
- Page End:
- 107738
- Publication Date:
- 2016-11-11
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c6ra24560a ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 221.xml