Specific recognition of proteins and peptides via controllable oriented surface imprinting of boronate affinity-anchored epitopes.

Molecularly imprinted polymers (MIPs) are chemically synthesized materials mimicking the recognition of antibodies towards antigens. Epitope imprinting has been an effective strategy, making imprinting of proteins flexible to a great extent. However, so far there is apparently a lack of facile and versatile epitope imprinting approaches. Herein, we present a new method called controllable oriented surface imprinting of boronate affinity-anchored epitopes. In this method, a C-terminus nonapeptide epitope was glycated and anchored as a template onto a boronic acid-functionalized substrate, followed by controllable oriented surface imprinting via the polycondensation of multiple silylating reagents containing functionalities capable of interacting with the epitope. The developed imprinting approach allowed for precise control of the thickness of the imprinting layer through adjusting the imprinting time, generating excellent binding properties. This method was verified to be versatile and efficient. Thus, it could greatly facilitate the preparation of MIPs for specific recognition of proteins and peptides.