Discussions

Numerous therapeutic proteins and peptides, including clotting factors, growth factors, hormones, enzymes, and antibodies, have been created in recent decades for a range of purposes. When compared to their natural equivalents, these proteins consistently exhibit comparable pharmacokinetic characteristics. Unfortunately, their low molecular mass causes terminal half-lives to be considerably less than a day, which severely restricts the range of therapeutic uses for them. In this instance, half-life extension techniques have played a crucial role in the creation of numerous biotherapeutics.

N- or O-glycosylation, which happens through posttranslational changes for many therapeutic glycoproteins, has significant effects on half-life and in vivo efficacy. Furthermore, the activity and binding characteristics of the proteins might also be impacted by glycosylation based half-life extension. In biochemistry research, the half-life extension method based on glycosylation has been widely used.