Glycosylation
The attachment of sugar molecules (glycans) to a peptide or protein. Glycosylation affects protein folding, stability, and biological activity. It is an important post-translational modification for many naturally occurring and recombinant therapeutic peptides.
Technical Context
Glycosylation involves attachment of sugar chains (glycans) to asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycans affect protein folding, stability, solubility, half-life, and immunogenicity. For recombinant therapeutic peptides produced in mammalian cell systems, glycosylation patterns depend on the host cell type and culture conditions, which is why glycosylation consistency is a major quality concern for biological products. Glycosylation differences can affect biosimilar comparability assessments. Some naturally glycosylated hormones (FSH, LH, TSH, hCG) require mammalian cell production to achieve appropriate glycosylation patterns.