Molecular imprinting technology has gained increasing attention and application in protein adsorption and separation. Bacterial growth on the imprinted material would reduce the adsorption selectivity of the imprinted cavity, contaminate the isolation products and shorten the service life of the material. To solve the above problems, carrier materials with dual antibacterial ability are constructed for the first time and novel surface protein imprinted microspheres (GO-PEI/MXene@MIPs) are manufactured. Thanks to the large exterior surface area, the saturation adsorption amount of GO-PEI/MXene@MIPs reaches 312.63 mg/g with an imprinting factor (IF) value of 3.16 within 90 min. Meanwhile, this imprinted material also exhibits a high ability to separate real samples as well as reusability. In addition, this material has excellent broad-spectrum antibacterial effects, which will significantly extend its service life in real-world environments. This study provides a feasible solution for the application of surface protein imprinted materials in real-world environments.

At present, the development of high-performance protein imprinted materials is still a research hotspot in the field of protein imprinting. Herein, anti-protein adsorption segment (CBMA)-assisted self-driven BSA surface imprinted fibers MTCFs@SIP@CBMA with high recognition selectivity are pioneered using the strategies of combining magnetic nanomaterial surface imprinting technique with amino-Michael addition. The special structure of the carrier MTCFs endows MTCFs@SIP@CBMA with magnetic performance and self-driven adsorption performance, which simplifies the separation process while improving the adsorption capacity and accelerating the adsorption rate. The adsorption capacity for BSA reached 395.26 mg/g within 30 min. The introduction of CBMA segments on the surface after imprinting by amino-Michael addition makes its polymer chain length and position controllable. Under the strongest anti-nonspecific adsorption effect, MTCFs@SIP@CBMA exhibit excellent specific identification to BSA from mixed proteins. Additionally, MTCFs@SIP@CBMA show considerable reusability. Therefore, MTCFs@SIP@CBMA are expected to be applied in efficient separation of proteins in biological samples.