Synthesis of a molecularly imprinted polymer using MOF-74(Ni) as matrix for selective recognition of lysozyme

A molecularly imprinted polymer and metal organic framework were combined to prepare protein imprinted material. MOF-74(Ni) was used as a matrix to prepare surface-imprinted material with lysozyme as a template and polydopamine as an imprinting polymer. MOF-74(Ni) not only provides a large surface a...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2020-10, Vol.412 (26), p.7227-7236
Main Authors: Li, Jie, Ma, Miaoxia, Zhang, Chenhui, Lu, Rui, Zhang, Lingyi, Zhang, Weibing
Format: Article
Language:English
Subjects:
Adsorption
Analysis
Analytical Chemistry
Biochemistry
Bovine serum albumin
Characterization and Evaluation of Materials
Chelation
Chemical synthesis
Chemistry
Chemistry and Materials Science
Electrophoresis, Polyacrylamide Gel
Food Science
Identification and classification
Immobilization
Imprinted polymers
Laboratory Medicine
Lysozyme
Metal-organic frameworks
Methods
Microscopy, Electron, Scanning
Microscopy, Electron, Transmission
Molecular Imprinting
Monitoring/Environmental Analysis
Muramidase - metabolism
Nickel
Polymers
Polymers - chemistry
Properties
Proteins
Research Paper
Ribonuclease A
Serum albumin
Spectrometry, X-Ray Emission
Surface chemistry
Target recognition
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Summary:A molecularly imprinted polymer and metal organic framework were combined to prepare protein imprinted material. MOF-74(Ni) was used as a matrix to prepare surface-imprinted material with lysozyme as a template and polydopamine as an imprinting polymer. MOF-74(Ni) not only provides a large surface area (150.0 m 2 /g) to modify the polymer layer with more recognition sites ( Wt (Ni) = 42.24%), but also facilitates the immobilization of lysozyme by using the chelation between Ni 2+ of the MOF-74(Ni) and protein. The thin polydopamine layer (10 nm) of the molecularly imprinted material (named MOF@PDA-MIP) enables surface imprinting. Benefiting from the thin polymer layer, MOF@PDA-MIP reached adsorption equilibrium within 10 min. The maximum adsorption capacity reaches 313.5 mg/g with the highest imprinting factor (IF) of 7.8. The specific recognition sites can distinguish target lysozyme from other proteins such as egg albumin (OVA), bovine serum albumin (BSA) and ribonuclease A (RNase A). The material was successfully applied to separation of lysozyme from egg white. Graphical abstract
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-020-02855-7