Construction of high-performance glycoprotein molecularly imprinted polymers using boronic acid-containing imidazolium ionic liquid monomer and UiO-66@wood sponge composite carrier

Glycoproteins are essential in biological systems, yet their complex structures and diverse glycosylation patterns present challenges for efficient and specific recognition. Herein, molecularly imprinted polymers (MIPs) with high selectivity and adsorption capacity for glycoproteins were developed using two synergistic strategies. One strategy was to synthesize a boronic acid-containing ionic liquid (PBA-IL) functional monomer that combines long-range non-covalent interactions with short-range covalent bonds, enhancing the interaction modes with ovalbumin (OVA) to improve imprinting efficiency. The other strategy entailed constructing a composite carrier with high specific surface area (50.3 m 2 /g) and abundant active sites by in-situ growth of UiO-66 metal–organic framework crystals on a wood-derived cellulose sponge (WCS). This composite (WCS@UiO-66) was utilized in a template immobilization method combined with surface imprinting technique (TIM-SIT) to prepare the MIPs (WCS@UiO-66@MIPs). Molecular simulations indicated that PBA-IL formed stronger interactions with OVA compared to traditional monomer. Based on these characteristics, the WCS@UiO-66@MIPs achieved rapid adsorption equilibrium within 40 min, exhibiting surprisingly high adsorption capacity (up to 571  mg g −1 ) and recognition ability (imprinting factor of 5.09) for OVA. The competitive adsorption experiments also demonstrated the efficient extraction of OVA from biological samples by WCS@UiO-66@MIPs, confirming its exceptional specificity. Additionally, the osmotic separation experiments revealed that WCS@UiO-66@MIPs achieved a selective permeation factor of up to 7.68 for OVA in a binary protein mixture, further demonstrating their potential for large-scale continuous separation processes. Therefore, this work provides a promising strategy for the efficient and specific recognition of glycoproteins, advancing their application in biotechnology and analytical chemistry.