An antifouling electrochemical biosensor based on a protein imprinted hydrogel for human immunoglobulin G recognition in complex biological media

We reported the construction of a specific and long-term antifouling biosensor interface based on a protein imprinted hydrogel for sensitive analysis of human immunoglobulin G (IgG) in complex biological media. The protein imprinted hydrogel was synthesized via a free radical polymerization reaction between a functional monomer of acrylamide and template protein IgG, with the aid of an initiator, a promoter, and a temperatureresponsive monomer. The synthesized hydrogel interface effectively reduced nonspecific protein adsorption and undesired cell adhesion, verified by electrochemical tests and fluorescence images. The proposed biosensor quantified the target IgG in a complex biological sample with high sensitivity and selectivity, resulting from good antifouling properties and analytical specificity toward the target. The response range of the reported hydrogelbased biosensor toward IgG was 0.5 - 200.0 ng/mL with a limit of detection of 0.03 ng/mL (S/N = 3). Notably, the developed biosensor could detect the target in a complex biological serum sample.

Automated summary

A specific and long-term antifouling biosensor interface was constructed based on a protein imprinted hydrogel for sensitive analysis of human immunoglobulin G (IgG) in complex biological media. The biosensor showed high sensitivity and selectivity in quantifying target IgG in complex biological samples, with a response range of 0.5 - 200.0 ng/mL and a limit of detection of 0.03 ng/mL (S/N = 3).