Related Experiment Video
Updated: Mar 21, 2026

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics DCAF
Published on: September 17, 2019
The Highly Evolvable Antibody Fc Domain
Hye In Park1, Hyun Woung Yoon1, Sang Taek Jung1
1Department of Bio and Nano Chemistry, Kookmin University, Seoul 136-702, Korea.
Abstract:
The Fc region of the IgG antibody recruits immune leukocytes or serum complement molecules, which in turn triggers the clearance of defective cells such as tumor cells or infected cells. In addition, the Fc region is crucial for the prolonged serum persistence of circulating IgG antibodies through an intracellular trafficking and recycling mechanism. Recently, the utility of antibody Fc has been further expanded to include a new class of antigen-binding scaffolds. This review presents the recent progress in the field of antibody Fc engineering and highlights new biomolecular, cellular, and evolutionary approaches to overcome the limitations of conventional monoclonal therapeutic antibodies by engineering the antibody Fc domain.
Related Concept Videos
Antibody Structure
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Antibody Actions
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Cross-reactivity
Affinity and Avidity

