Glycosylation is the attachment of carbohydrates to the backbone of a protein through an enzymatic reaction. It plays a critical role in determining protein structure, function and stability. A protein that is glycosylated is known as a glycoprotein. The two most common types of protein glycosylation are known as N-glycosylation and O-glycosylation.
A new study by researchers at Boston University Chobanian & Avedisian School of Medicine set out to improve on existing methods to identify glycopeptides and found that conventional mass spectrometry methods were sufficient to identify peptides with one glycan (essential biomolecules serving structure, energy storage and system regulatory purposes) but that an additional step is necessary for identifying peptides with two or more glycans.
Because one protein can carry many glycans, it can be difficult or impossible to generate peptides that only carry one glycan. The ability to identify peptides with multiple glycans is key to defining different glycoforms of the protein to understand its biological function and the role in the disease.
Due to the lack of information about glycoproteins and how they change during development and disease, corresponding author Manveen K. Sethi, Ph.D., research assistant professor of biochemistry & cell biology, believes they may be missing promising therapeutic avenues. “A more thorough and specific understanding of how glycosylation affects disease, specifically site-specific alterations, may