Issue 6, 2019

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

Abstract

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.

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

Supplementary files

Article information

Article type
Edge Article
Submitted
19 sept. 2018
Accepted
30 nov. 2018
First published
03 déc. 2018
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2019,10, 1831-1835

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

R. Xing, Y. Ma, Y. Wang, Y. Wen and Z. Liu, Chem. Sci., 2019, 10, 1831 DOI: 10.1039/C8SC04169E

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