Developing synthetic and analytical tools to study the effect of modifications on glycans binding preferences

Modifications of complex glycans and proteins govern their binding preferences and biological activities. Evaluating the effect of sulfation and sialylation on glycans interaction is not straightforward because obtaining modified complex glycans in sufficient quantity is not easy. In addition, those interactions are too weak to quantify using standard bioanalytical tools.

We develop sysnthetic methods for the synthesis of complex glycands and use label-free electrochemical tools for studying the effect of glycans modifications on interaction preferences. Assembly of complex glycans on electrodes enables studying glycan interaction with proteins, metal ions and even enzymatic processed by the electrochemical impedance spectroscopy. The use of surface chemistry tools allows utilizing only minute quantities of complex glycans while the electrochemical signal enables label-free sensing of even very weak interactions by following the changes in the glycan layer hence differs significantly from classic analytical methods.

I will present our new approach for expediting the synthesis of both glycans and peptides and demonstrate how this synthetic advantage leads to new findings.