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