Abstract

Novel PEGylated thermo-sensitive bionic magnetic core-shell structure molecularly imprinted polymers (PMMIPs) for the specific adsorption and separation of bovine serum albumin (BSA) were obtained via a surface-imprinting technique. X-ray diffraction (XRD), scanning electron microscopy (SEM), transmission electron microscopy (TEM), vibrating sample magnetometry (VSM), fourier transform infrared spectrometry (FT-IR), thermal gravimetric analysis (TGA), and specific surface area (BET), were adopted to demonstrate that novel PMMIPs were successfully synthesized. Subsequently, the prepared PMMIPs were used as the extractor for BSA and were combined with magnetic solid-phase extraction. The concentrations of BSA were detected by UV-vis spectrophotometry at 278 nm. The maximum adsorption capacity of the PMMIPs was 258 mg g−1, which is much higher than that of non-imprinted polymer (PMNIPs). PMMIPs showed favorable selectivity for BSA against reference proteins, i.e., bovine hemoglobin, ovalbumin and lysozyme. PMMIPs were further used to recognize BSA in protein mixtures, milk, urine and sewage, these results revealed that approximately 96% of the ideal-state adsorption capacity of PMMIPs for BSA was achieved under complicated conditions. Regeneration and reusability studies demonstrated that adsorption capacity loss of the PMMIPs was not obvious after recycling for four times. Facile synthesis, excellent adsorption property and efficient selectivity for BSA trapping are features that highlight PMMIPs as an attractive candidate for biomacromolecular purification.

Highlights

  • Proteins are important biomarkers for certain diseases, health conditions, environmental monitoring, and food quality

  • The overall synthetic route of PMMIPs and our protein captured and released strategy are drawn in Scheme 1

  • LCST, which would promote template molecule escape from the imprinted cavities. These results indicated that the PMMIPs (PMNIPs) displayed excellent thermo-sensitive, which was significant for absorption and desorption of template molecule

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Summary

Introduction

Proteins are important biomarkers for certain diseases, health conditions, environmental monitoring, and food quality. The detection of biomarker proteins has become increasingly important, meaning that the construction of biosensors for such biomarker targets has become increasingly important. For the past few years, the molecular imprinting technique (MIT) has received extensive attention in protein separation for its specific identification, efficient selectivity and strong affinity for template molecules [1,2]. Imprinting is an effective separation method that creates artificial affinity binding sites in polymeric matrices [3]. Imprinted polymers (MIPs) are synthesized by copolymerization of cross-linkers and functional monomers. Template molecules should be added before the polymerization process and removed afterwards; this allows the functional groups, size, and shape of template molecules to become memorized within the matrix, leaving behind specific recognition cavities [4]. MIPs have advantages of structural predictability and recognition specificity [5]

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