(771a) Sugar-Coating the Answers to Virus Binding: Glycocalyx-Mimetic Interfaces

The glycocalyx is a membranous structure composed of glycoproteins and carbohydrate residues. This sugary forest that sheaths our cells is responsible for protecting us from pathogen invasions and forms a crucial component of our cells’ immune machinery. Virus-glycocalyx interactions are poorly understood and a detailed study of these interactions is hindered by the tendency of the native glycocalyx to collapse during in vitro studies. We have developed a bio-inspired model system for the glycocalyx to identify and understand physicochemical parameters that shape its interactions with viral pathogens. Like the native glycocalyx, our tunable surface engages in both specific and non-specific modes of viral binding. We have developed a library of carbohydrate-based polymer brushes, including mannose, glucose and galactose, which recapitulate the chemical complexity of the glycocalyx. Though our carbohydrate-functionalized surfaces are inert to non-specific protein adsorption, they recognized lectin. Spatially controlled immobilization of brushes helped us achieve precisely patterned presentation of lectins and viruses. In addition to specific affinity based interactions, we have also engineered non-specific electrostatically mediated interactions into our surface to elucidate the role of surface charge on viral binding. Our model surface is composed of positively charged affinity sites and polymerization initiation sites for the growth of polymer brushes bearing carbohydrate residues. By varying the ratio of affinity sites to initiation sites, we were able to observe changes in adsorption profiles of model proteins, influenza viruses and adenoviruses. Quartz crystal microbalance, scanning electron microscopy and fluorescence microscopy were employed to visualize these interactions and develop design rules for virus-resistant coatings