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Green synthesis of hydrophilic protein-imprinted resin with specific recognition of bovine serum albumin in aqueous matrix
- Source :
- Analytica Chimica Acta. 1033:213-220
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
Abstract
- The synthesis of biomacromolecule imprinted materials is a challenge with the bulkiness and instability of macromolecule, such as protein. A green strategy to prepare hydrophilic protein-imprinted resin (HPIR) was firstly developed using resorcinol and melamine as double functional monomers, hexamethylenetetramine instead of formaldehyde as crosslinker, water as solvent, and bovine serum albumin (BSA) as a dual-function template. BSA as dual-function template could not only act as template but also porogen in the preparation of HPIR. According to the adsorption experiments, the adsorption kinetics of BSA on HPIR obeyed pseudo-second-order adsorption kinetics and the equilibrium data were best described by Langmuir isotherm model. The adsorption capability was 44.3459 mg g−1 (25 °C), and the imprinted factor for binding BSA is 5.78. HPIR showed high adsorption capacity, fast mass transfer rate, and specific selectivity towards BSA in aqueous solvent. More importantly, HPIR can be applied to selectively adsorb target protein BSA in urine without the matrix interference of biological matrix, therefore, it is promising for HPIR to be applied to proteomics, diagnostics, and pharmaceutics.
- Subjects :
- Macromolecular Substances
Surface Properties
02 engineering and technology
Resorcinol
010402 general chemistry
01 natural sciences
Biochemistry
Analytical Chemistry
Molecular Imprinting
chemistry.chemical_compound
symbols.namesake
Adsorption
Environmental Chemistry
Particle Size
Bovine serum albumin
Spectroscopy
Aqueous solution
Molecular Structure
biology
Water
Langmuir adsorption model
Serum Albumin, Bovine
021001 nanoscience & nanotechnology
0104 chemical sciences
Solvent
Resins, Synthetic
chemistry
biology.protein
symbols
Hexamethylenetetramine
0210 nano-technology
Melamine
Hydrophobic and Hydrophilic Interactions
Nuclear chemistry
Subjects
Details
- ISSN :
- 00032670
- Volume :
- 1033
- Database :
- OpenAIRE
- Journal :
- Analytica Chimica Acta
- Accession number :
- edsair.doi.dedup.....0979339fccc31efa0c6777c3bade270f