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modified—meaning that after they’re made, they're
decorated with complex structures that change how they
behave.

Glycosylation is one of the most important of these
modifications.

It’s the process of attaching sugars—called glycans—to
specific amino acids on the protein surface. These glycans
shape the protein’s folding, protect it from degradation, and
serve as biochemical signposts for how it should be
handled inside the body.

In monoclonal antibodies, for example, glycosylation
affects everything from the drug’s half-life in the
bloodstream to its ability to trigger immune effector
functions like antibody-dependent cellular cytotoxicity
(ADCC). In enzyme replacement therapies, it dictates
whether a cell will recognize, internalize, or ignore the
therapeutic protein altogether.

In short: glycosylation matters.

But it matters even more when it goes wrong.

The Immune System Reads Sugar Like a Fingerprint

Here’s the problem: glycosylation is not template-driven.
There is no DNA code that ensures a glycoprotein made in
one batch will carry the exact same sugars as the next.

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