In recent years, there has been growing interest in engineering Fc proteins and modifying the glycosylation of antibodies to enhance their therapeutic potential. Fc proteins are composed of two heavy chains and two light chains, each containing a variable (V) and a constant (C) region. The Fc region of antibodies is located at the C-terminal end of the heavy chain and is responsible for mediating effector functions. Fc proteins from different species can differ in their amino acid sequence and glycosylation patterns, leading to variations in their FcR binding and functional activity.

Fc Protein And Glycoengineered Antibodies involves modifying the amino acid sequence of the Fc region to enhance or reduce its effector functions. For example, the substitution of an asparagine residue at position 297 (N297) of the Fc region with other amino acids can abolish or enhance the binding of Fc to FcRs or complement. N297 is the site of N-linked glycosylation, which plays a critical role in modulating Fc function. The addition of a glycan at N297 can increase the binding of Fc to FcγRIIIa and enhance ADCC.

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