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Constructing High-Recognition Protein-Imprinted Materials Using "Specially Designed" Block Macromolecular Chains as
Wenqi Song1, Liwei Qian2,3, Yuxuan Yang2
1Xi' an Key Laboratory of Advanced Photo-electronics Materials and Energy Conversion Device, School of Science, Xijing University, Xi'an 710123, PR China.
ACS Applied Materials & Interfaces
|November 4, 2021
Summary
A novel block macromolecularly functional monomer and crosslinker (MFM) effectively imprinted bovine serum albumin (BSA), preserving protein structure and achieving high adsorption capacity. This method enhances protein imprinting technology for superior recognition materials.
Area of Science:
- Biomaterials Science
- Polymer Chemistry
- Analytical Chemistry
Background:
- Protein imprinting requires monomers that stabilize protein structure during the imprinting process.
- Existing micromolecular monomers can denature proteins, limiting imprinting efficiency.
- Macromolecularly functional monomers (MFMs) offer a promising approach for protein imprinting.
Purpose of the Study:
- To synthesize and evaluate a novel block MFM for creating high-recognition bovine serum albumin (BSA)-imprinted microspheres.
- To compare the performance of the block MFM with a micromolecularly functional monomer (MIM).
- To investigate the impact of zwitterionic functional groups within the MFM on protein imprinting.
Main Methods:
- Synthesis of a block MFM via reversible addition-fragmentation chain-transfer (RAFT) polymerization.
- Fabrication of SiO2@MPS@MIPs-MFM microspheres using a surface imprinting strategy.
- Characterization using circular dichroic (CD) spectroscopy, batch rebinding experiments, scanning electron microscopy (SEM), and transmission electron microscopy (TEM).
Main Results:
- The block MFM maintained the native structure of BSA, unlike the MIM which caused denaturation.
- BSA-imprinted microspheres fabricated with the block MFM exhibited a maximum adsorption capacity of 314.9 mg g⁻¹ and an imprinting factor of 4.02.
- The presence of zwitterionic groups in the MFM enhanced specific protein rebinding.
- A thin imprinted layer (approx. 15 nm) facilitated rapid adsorption equilibrium within 120 minutes.
- The material demonstrated excellent selectivity and recognition in mixed protein solutions and extracted BSA from biological samples.
Conclusions:
- The developed block MFM is superior to traditional MIMs for protein imprinting, preserving protein structure and enhancing binding capacity.
- The block MFM design, incorporating zwitterionic groups, improves specific protein recognition and selectivity.
- This novel approach provides a versatile platform for designing high-performance protein-imprinted materials for various applications, including biological sample analysis.
