Glycosylation of Therapeutic Protein

After years of intensive research, we have accumulated considerable experience in therapeutic protein research. Increasing evidence revealed that protein drugs play an essential role in numerous diseases, which provides a new perspective for the applications of protein drugs. Creative Biolabs is a world-leading service provider and is fully committed to providing high-quality and low-cost services to advance research on protein glycosylation.

In the past decade, much attention has been focused on protein drugs that are emerging as safe vehicles for targeted disease therapeutics. But their development and application are often limited due to their pharmacological properties. Increasing evidence showed that glycosylation can improve the therapeutic effect of biopharmaceuticals.

Fig.1 Glycosylation of therapeutic proteins. (Walther, 2021)

Types of Glycosylation of Therapeutic Proteins

The stability of the therapeutic protein is the basis of its transportation, storage, and therapeutic response. Glycosylation plays a ponderable role in increasing protein stability. Many therapeutic proteins can undergo different types of glycosylation. Among the various types, O-linked glycosylation and N-linked glycosylation are two typical types. Because the protein needs to be folded after glycosylation, there is a difference in the activity or stability of the glycosylated protein.

Effects of Glycosylation

• Protein molecular stability

Glycans are very important for the integrity of glycoproteins. Some results demonstrated that glycosylation increases the thermal stability of proteins, prevents proteolysis, improves solubility, and inhibits protein aggregation. These functions lay the foundation for the development and optimization of therapeutic glycoproteins. What's more, engineered glycosylation was proven to simultaneously optimize drug molecule stability and pharmacodynamics, thereby the design of protein therapy with optimized efficacy can be achieved.

• Pharmacokinetics and serum half-life

The in vivo efficacy of a drug usually depends on the pharmacokinetic behavior of the drug, including clearance, serum half-life, and critical concentration. Glycosylation also has an important influence on the pharmacokinetics and half-life of protein drugs. Many studies have revealed that compared with non-glycosylated forms, highly glycosylated proteins have a longer serum half-life, lower sensitivity to proteolysis, higher thermal stability, and better effects.

Assessment of Therapeutic Proteins

The glycans attached to the therapeutic glycoprotein will Significantly affect the product quality and efficacy. Therefore, it is very important to analyze and control the glycan part of the therapeutic protein in the product life cycle. A variety of high-efficiency measurement methods have been developed including high-performance liquid chromatography (HPLC) mass spectrometry (MS), high-performance anion-exchange chromatography (HPAEC-PAD) with pulsed amperometric detection, and capillary electrophoresis (CE). It is worth noting that the lectin microarray is emerging as a supplementary tool for therapeutic glycoprotein assessment.

In recent years, glycosylation of therapeutic proteins has gradually become a hot spot. As a leader in this field, Creative Biolabs provides the most effective techniques to promote the progress of your project in a short time. In addition to sophisticated technology, our experienced experts also offer the best solution for your therapeutic proteins research. Please feel free to contact us for more detailed information.

Reference

1. Walther, R.; Zelikin, A.N. Chemical (neo) glycosylation of biological drugs. Advanced Drug Delivery Reviews. 2021.

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