Glycoproteomics

Glycoproteomics is the large-scale study of glycoproteins — proteins that carry carbohydrates, called glycans, covalently attached to their amino acid side chains. As a subdiscipline of proteomics, it works to understand the structure, function, and interactions of these molecules and what they reveal about biology and disease.

A hidden layer of information

Glycans come in several classes: N-linked variants attach to asparagine residues, O-linked variants attach to serine or threonine, and glycosaminoglycans form long, unbranched polysaccharide chains. These structures are not decoration. They substantially shape how a protein behaves — altering its location within the cell, enabling or disabling its interactions with other molecules, and even determining its half-life in circulation.

In the immune system, glycans help cells recognize pathogens and mediate the communication that regulates an immune response. They are central to cell adhesion and signaling, including the formation of the extracellular matrix — the network of proteins and carbohydrates that gives cells and tissues their structural support.

Why it matters for medicine

Aberrant glycosylation patterns are implicated in cancer progression, in neurodegenerative conditions such as Alzheimer’s and Parkinson’s, and in congenital disorders of glycosylation. Reading those patterns is precisely the signal InterVenn Biosciences set out to decode — using AI to turn glycan biology into earlier, more accessible cancer detection.