Precise generation of selective surface-confined glycoprotein recognition sites
File(s)
Accepted version
Author(s)
Mitchell, Philippa
Tommasone, Stefano
Angioletti-Uberti, Stefano
Bowen, James
Mendes, Paula M
Type
Journal Article
Abstract
Since glycoproteins have become increasingly recognized as key players in a wide variety of disease processes, there is an increasing need for advanced affinity materials for highly selective glycoprotein binding. Herein, for the first time, a surface-initiated controlled radical polymerization is integrated with supramolecular templating and molecular imprinting to yield highly reproducible synthetic recognition sites on surfaces with dissociation constants (KD) in the low micromolar range for target glycoproteins and minimal binding to nontarget glycoproteins. Importantly, it is shown that the synthetic strategy has a remarkable ability to distinguish the glycosylated and nonglycosylated forms of the same glycoprotein, with a >5-fold difference in binding affinity. The precise control over the polymer film thickness and positioning of multiple carbohydrate receptors plays a crucial role in achieving an enhanced affinity and selectivity. The generated functional materials of unprecedented glycoprotein recognition performance open up a wealth of opportunities in the biotechnological and biomedical fields.
Date Issued
2019-06-17
Date Acceptance
2019-05-12
Citation
ACS Applied Bio Materials, 2019, 2 (6), pp.2617-2623
ISSN
2576-6422
Publisher
American Chemical Society (ACS)
Start Page
2617
End Page
2623
Journal / Book Title
ACS Applied Bio Materials
Volume
2
Issue
6
Copyright Statement
© 2019 American Chemical Society. This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Applied Bio Materials, after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acsabm.9b00289.
Publication Status
Published
Date Publish Online
2019-05-13