Issue 9, 2015

Selective glycoprotein detection through covalent templating and allosteric click-imprinting

Abstract

Many glycoproteins are intimately linked to the onset and progression of numerous heritable or acquired diseases of humans, including cancer. Indeed the recognition of specific glycoproteins remains a significant challenge in analytical method and diagnostic development. Herein, a hierarchical bottom-up route exploiting reversible covalent interactions with boronic acids and so-called click chemistry for the fabrication of glycoprotein selective surfaces that surmount current antibody constraints is described. The self-assembled and imprinted surfaces, containing specific glycoprotein molecular recognition nanocavities, confer high binding affinities, nanomolar sensitivity, exceptional glycoprotein specificity and selectivity with as high as 30 fold selectivity for prostate specific antigen (PSA) over other glycoproteins. This synthetic, robust and highly selective recognition platform can be used in complex biological media and be recycled multiple times with no performance decrement.

Graphical abstract: Selective glycoprotein detection through covalent templating and allosteric click-imprinting

Supplementary files

Article information

Article type
Edge Article
Submitted
07 6 2015
Accepted
15 6 2015
First published
17 6 2015
This article is Open Access

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

Chem. Sci., 2015,6, 5114-5119

Author version available

Selective glycoprotein detection through covalent templating and allosteric click-imprinting

A. Stephenson-Brown, A. L. Acton, J. A. Preece, J. S. Fossey and P. M. Mendes, Chem. Sci., 2015, 6, 5114 DOI: 10.1039/C5SC02031J

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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