Molecular imprinting is a chemical strategy to create synthesized materials that can specifically bind target molecules.Molecularly imprinted polymers (MIPs),also called artificial antibodies or plastic antibodies,provide similar binding properties and meanwhile overcome the disadvantages of antibodies,such as poor stability and high cost.Molecular imprinting of proteins is of great importance but remains a challenge.Particularly,universal and rapid methodologies are limited.Here we report a general strategy for facile imprinting of glycoproteins: boronate affinity-based molecular imprinting.Boronate affinity is a unique chemisty that boronic acids covalently interact with cis-diol-containing molecules such as sugars or glycoproteins to form stable cyclic esters in an alkaline aqueous solution while the boronate esters dissociate when the environmental pH is switched to acidic.We first developed a general and facile approach,photolithographic boronate affinity molecular imprinting.The approach relied on boronic acid-based UV-initiated polymerization,in which a boronic acid played essential roles.MIP thin-layer arrays were produced using a photolithographic fabrication route.The generality of the approach was demonstrated with the successful imprinting of five distinct glycoproteins.The approach showed fast speed and the potential for easy mass production.The prepared MIP arrays exhibited several highly attractive features that are beyond normal expectation,particularly superb tolerance for interference and the applicability to a wide range of sample pH.The feasibility for real-world applications was demonstrated with the analysis of trace glycoproteins in human serum.However,this approach was only applicable for 2D imprinting.To overcome such a limitation,we further developed a new approach,controllable oriented imprinting.Target molecules were first immobilized onto a boronic acid-functionalized substrate (2D or 3D),then a biocompatible layer was fabricated around the target molecules.Once the target molecules were removed,3D cavities complementary to the shape of the template were formed,within which boronic acids provided the major binding force.By using this approach,several typical glycoproteins such as HRP,RNase B and transferrin,have been successfully imprinted in monolithic capillaries.The molecularly imprinted monolithic capillaries exhibited excellent specificity towards the targets.Specific extraction of transferrin from human serum with a transferrin-imprinted monolithic capillary was demonstrated.As glycoproteins are of biological and clinical importance,we foresee the proposed strategy and approaches would find promising applications in multiple areas such as proteomic analysis and diagnostic analysis.