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Preparation of lysozyme-imprinted nanoparticles on polydopamine-modified titanium dioxide using ionic liquid as a
Zhongliang Zhao1,2, Caihong Zhu1, Qianping Guo1
1College of Chemistry, Chemical Engineering and Materials Science, Orthopaedic Institute, Medical College, Soochow University Suzhou China.
RSC Advances
|May 6, 2022
Summary
Ionic liquids stabilize proteins during molecular imprinting, enabling efficient recognition. This study developed titanium dioxide nanoparticles with lysozyme-imprinted sites for selective protein separation.
Area of Science:
- Materials Science
- Biotechnology
- Analytical Chemistry
Background:
- Protein molecular imprinting is key for recognition and separation.
- Maintaining protein structural stability during imprinting is a challenge.
- Ionic liquids (ILs) can stabilize proteins, aiding imprinting.
Purpose of the Study:
- To develop lysozyme-imprinted titanium dioxide (TiO2) nanoparticles (TiO2@Lyz-MIPs) for selective lysozyme recognition and separation.
- To investigate the role of polydopamine (PDA) modification and ILs in improving imprinting efficiency.
- To optimize the preparation of TiO2@Lyz-MIPs for enhanced adsorption capacity and selectivity.
Main Methods:
- Free radical polymerization of HEA and PEGDMA on PDA-modified TiO2 nanoparticles.
- Utilized choline dihydrogen phosphate (chol dhp) as an IL stabilizer for lysozyme.
- Optimized monomer concentration, monomer-to-crosslinker ratio, and IL concentration.
Main Results:
- Successfully prepared TiO2@Lyz-MIPs with an imprinting factor of 4.40 under optimal conditions.
- Achieved a maximum adsorption capacity of 120 mg g-1, over four times higher than non-imprinted polymers.
- Demonstrated selective separation of lysozyme from diluted egg white, a complex protein mixture.
Conclusions:
- The developed TiO2@Lyz-MIPs exhibit effective recognition cavities for lysozyme.
- The use of ILs as stabilizers enhances protein imprinting and recognition capabilities.
- This approach offers a promising strategy for developing MIPs for efficient protein separation.
