Fc-FUSION PROTEINS; STRUCTURAL MODIFICATIONS AND HORMONAL THERAPY
Manoj G. Tyagi*
ABSTRACT
In the recent years, IgG-based therapeutics and antibodies have gained significant importance for the treatment of a wide range of diseases, including autoimmunity and inflammation, cancers, cardiovascular and infectious diseases and transplantation medicine. Approximately 370 IgG-based therapeutics are approved for clinical use or are under development for many diseases lacking proper treatment options. On the other hand, the Fraction crystallizable (Fc) -based drugs demand additional considerations because interactions between the Fc domain and its receptors have immunological consequences. These interactions raise concerns about the long-term use of these products, which are often employed to treat chronic conditions. Degradation of recombinant proteins in culture is a common and serious problem. Degradation of most proteins, including recombinant monoclonal antibodies and fusion proteins, may be attributed to host cell-derived proteases, which may be very site specific or have a broad substrate range. Heterodimeric Fc fragments, which can present the fusion partner as native-like monomeric or heterodimeric forms, represent a promising scaffold for the next generation of Fc-fused proteins and cytokines. This review article encompasses the challanges for better potential candidates for therapeutics using Fc fusion technology.
Keywords: Fc fusion, antibodies, heterodimeric, protein, therapeutics
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