Our latest work in the design of new materials to mimic complex glycan function and to inhibit bacterial toxins has been published in ACS Macro Letters. We have previously shown that synthetic polymers bearing carbohydrates in specific orientations or densities on polymer chains can give rise to increased affinity towards bacterial lectins (toxins) and may have application as decoys to prevent infection. However, many glycopolymers are rather basic simply having lots of glycans on a flexible polymer chain. In this work, we collaborated with Prof Filip du Prez (Gent, Belgium) using their thiolactone chemistry to enable us to introduce two functional units per repeat unit of the polymer. This was advantageous as it enabled us to mimic how GM-1 - a glycolipid on our cells - presents its glycans, but in a very simple manner. Using this, we made a library of glycopolymers with either 2 glycans or a hydrophobic unit. Using a combination of inhibitory assays and biolayer interferometry we unraveled the crucial design features to obtain highly active inhibits of lectin binding. This approach shows that moving from 'boring' homo-glycopolymers to those of increased complexity may help guide the development of materials to address the spread of infection.

Read the paper here

Double-Modified Glycopolymers from Thiolactones to Modulate Lectin Selectivity and Affinity