Fc Protein and Glycoengineered Antibodies Research to Grow Rapidly

Fc Protein and Glycoengineered Antibodies

Fc Protein And Glycoengineered Antibodies are a novel class of therapeutic antibodies that can be used in a variety of diseases. They are highly efficient, and are able to deliver targeted therapies. However, they can be associated with high side effects and pharmacokinetic concerns. Therefore, the development of Fc protein and glycoengineered antibodies is a key strategic priority for pharmaceutical companies.

The main objective of Fc Protein And Glycoengineered Antibodies research is to develop a new generation of antibody that can be used in the treatment of various diseases. This is done by combining innovative strategies and techniques to improve the safety, functionality, and efficacy of these antibodies.

Glycosylation of proteins influences biological activity, protein conformation, stability, solubility, secretion, pharmacokinetics and antigenicity. It is also a key quality attribute of the antibody, and efficient and quantitative glycan analysis is critical to the development and production of therapeutic IgGs.

There are many reasons for the increasing interest in manipulating the carbohydrate components of the therapeutic antibody and Fc fusion protein, including the need to optimize antibody function and to develop novel antibody therapies. This is particularly the case in the context of precision medicine, where antibodies are designed to specifically target and inhibit specific cellular targets, such as cancer cells.

Several studies have shown that the N-glycans of therapeutic IgG antibodies are a crucial influence on the biological activity and pharmacokinetics of these compounds. These glycans can either contribute to a therapeutic effect through enhanced ADCC and CDC activity or can be a hazard by increasing the toxicity of the antibodies.

In particular, the N-glycans of the Fc region have been found to play an essential role in the mechanism of action of most clinically applicable antibodies. They are critical for the activation of Fcg receptors on leukocytes and C1 component of complement, which is a major contributor to therapeutic effector functions such as ADCC and CDC.

To address the impact of N-glycosylation on the structure and functionality of these antibodies, a number of different strategies have been developed in recent years. One of the most widely studied and promising approaches involves chemoenzymatic glycoengineering (glycosylation engineering) based on endoglycosidase-based glycosynthases, which can be used to modify the N-glycans of monoclonal antibodies and Fc fusion proteins in a controlled manner.

As a result, the control of N-glycosylation in recombinant antibodies can be manipulated without any additional protein modifications, which could significantly reduce cost and increase the efficiency of glycosylation engineering. This has been demonstrated for therapeutic monoclonal antibodies as well as Fc fusion proteins, which are produced in yeast and other biotechnology platforms. Recently, in January 2022, Argenx SE, received approval from Ministry of Health, Labor, and Welfare of Japan for its VYVGART intravenous Fc receptor blocker for treating patients with generalized myasthenia gravis. 

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