Antibodies have been widely used for therapeutics and diagnosis due to their high specificity and affinity for the targets; development of antibodies has been extensively investigated in various fields. Once we obtain the genes encoding a monoclonal antibody, we can engineer various molecules using the antibody genes as a recognition element. However, it is not so far since we could understand how an antibody creates the specificity and affinity for the target from structural and energetic viewpoints. In this review, we firstly summarize three methods for biophysical characterization of antibody-antigen interactions. Second, we review our recent progresses on understanding how an antibody recognizes the target antigen from structural and energetic viewpoints. Finally, we discuss how we can create and improve the affinity of an antibody toward the target.
CITATION STYLE
Tsumoto, K. (2013). Dissection of antibody-antigen interactions for development of antibodies. Drug Delivery System, 28(5), 412–423. https://doi.org/10.2745/dds.28.412
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