Glycans (glycoproteins, glycolipids and proteoglycans) are ubiquitous. They are present in almost all cell surfaces, forming the glycocalyx, a fuzzy complex and crowded coat surrounding the external surface of cells. The glycocalyx is a complex and crowded environment in which, the glycocode is read (recognized) and translated by specific glycan-binding receptors. Through these molecular recognition events, glycans modulate various biological and physiological processes, such as, immune, and inflammatory responses, signalling and cellular adhesion processes, with strong impact in tumour growth and metastasis and in infection by pathogens.

Cracking how the glycocode is created and how it is recognized is crucial to understand or even predict the glycocode-modulated biofunctions, paving the way for developing new glycan-based therapies and diagnostic tools.

In this perspective, our research mission is to unravel the chemical and the molecular basis how specific enzymes create the glycocode and how it is read and translated by glycan-binding proteins (GBPs), contributing for the rational design and development of new treatments and diagnostic tools. To address our mission a chemical-structural and functional approach is pursued, which integrates complementary analytical, biophysical, and structural techniques sustained by chemoenzymatic synthesis and molecular biology protocols. NMR spectroscopy is the main structural technique to uncover glycans’ structure, catalysis, and recognition.