Click synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles with polydopamine coating for enrichment of trace glycoproteins. Issue 23 (11th November 2015)
- Record Type:
- Journal Article
- Title:
- Click synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles with polydopamine coating for enrichment of trace glycoproteins. Issue 23 (11th November 2015)
- Main Title:
- Click synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles with polydopamine coating for enrichment of trace glycoproteins
- Authors:
- Sun, Lixiang
Lin, Danhong
Lin, Guowei
Wang, Ling
Lin, Zian - Abstract:
- Abstract : Novel boronic acid-functionalized molecularly imprinted silica nanoparticles with polydopamine coating were prepared and applied to the recognition and enrichment of glycoproteins. Abstract : A facile strategy based on the synergistic effect of molecular imprinting and boronate affinity was proposed for glycoprotein imprinting. Polydopamine (PDA)-coated boronic acid-functionalized molecularly imprinted silica nanoparticles (MIPs) were prepared by the "thiol–ene" click reaction using SiO2 as the core, 3-acrylamidophenyl boronic acid (AAPBA) as the functional monomer, and horseradish peroxidase (HRP) as the glycoprotein template. A well defined core–shell structure of MIPs was obtained after self-polymerization of dopamine (DA) on the surface of HRP-immobilized silica nanoparticles (NPs). The polymerization conditions and adsorption behavior were investigated in detail in order to obtain the highest selectivity and binding capacity. Under the optimized conditions, the HRP-MIPs showed higher binding affinity towards HRP than non-imprinted nanoparticles (NIPs), and the corresponding adsorption capacity ( Q ) and imprinted factor ( α ) reached 0.58 μmol g −1 and 2.6, respectively. The specificity for HRP recognition was evaluated with a competitive experiment, and the results indicated that the HRP-MIPs had higher selectivity for the template. The good features of the HRP-MIPs facilitated selective isolation and enrichment of trace HRP from human serum. In addition,Abstract : Novel boronic acid-functionalized molecularly imprinted silica nanoparticles with polydopamine coating were prepared and applied to the recognition and enrichment of glycoproteins. Abstract : A facile strategy based on the synergistic effect of molecular imprinting and boronate affinity was proposed for glycoprotein imprinting. Polydopamine (PDA)-coated boronic acid-functionalized molecularly imprinted silica nanoparticles (MIPs) were prepared by the "thiol–ene" click reaction using SiO2 as the core, 3-acrylamidophenyl boronic acid (AAPBA) as the functional monomer, and horseradish peroxidase (HRP) as the glycoprotein template. A well defined core–shell structure of MIPs was obtained after self-polymerization of dopamine (DA) on the surface of HRP-immobilized silica nanoparticles (NPs). The polymerization conditions and adsorption behavior were investigated in detail in order to obtain the highest selectivity and binding capacity. Under the optimized conditions, the HRP-MIPs showed higher binding affinity towards HRP than non-imprinted nanoparticles (NIPs), and the corresponding adsorption capacity ( Q ) and imprinted factor ( α ) reached 0.58 μmol g −1 and 2.6, respectively. The specificity for HRP recognition was evaluated with a competitive experiment, and the results indicated that the HRP-MIPs had higher selectivity for the template. The good features of the HRP-MIPs facilitated selective isolation and enrichment of trace HRP from human serum. In addition, the stability and regeneration were also investigated, which indicated that the HRP-MIPs had excellent reusability. … (more)
- Is Part Of:
- Analytical methods. Volume 7:Issue 23(2015)
- Journal:
- Analytical methods
- Issue:
- Volume 7:Issue 23(2015)
- Issue Display:
- Volume 7, Issue 23 (2015)
- Year:
- 2015
- Volume:
- 7
- Issue:
- 23
- Issue Sort Value:
- 2015-0007-0023-0000
- Page Start:
- 10026
- Page End:
- 10031
- Publication Date:
- 2015-11-11
- Subjects:
- Chemistry, Analytic -- Periodicals
Analytical biochemistry -- Periodicals
Chemical laboratories -- Standards -- Periodicals
543.1905 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/AY ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c5ay02131f ↗
- Languages:
- English
- ISSNs:
- 1759-9660
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0897.103700
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1742.xml