mt9b00289_si_001.pdf (1021.68 kB)
Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites
journal contributionposted on 2019-05-13, 00:00 authored by Philippa Mitchell, Stefano Tommasone, Stefano Angioletti-Uberti, James Bowen, Paula M. Mendes
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.
glycoprotein bindingaffinity materialssupramolecular templatingdisease processesK Dmicromolar rangePrecise Generationpolymer film thicknessrecognition sitesglycoprotein recognition performanceSelective Surface-Confined Glycoprotein Recognition Sitescarbohydrate receptorsdissociation constantsnontarget glycoproteinstarget glycoproteinsbinding affinitynonglycosylated forms