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Antibody Affinity Maturation

By engineering antibodies with display technology, computer-aided design and site mutagenesis, 

various properties of the therapeutic antibody candidates can be improved with the purpose of enhancing their safety, 

efficacy and developability. 


Antibody Affinity Maturation


Antigen binding affinity is one of the most critical properties of a therapeutic antibody. Therefore, methods used for antibody affinity maturation, including random mutagenesis, targeted mutagenesis, chain shuffling and in silico approaches, are widely applied.

NBbiolab uses Computer-Based Modeling to generate a 3D structure of an antibody–antigen complex and predict mutation“hotspots”generate a large number of antibody variants with specific mutations. This, combined with Our State-of-the-Art Yeast Surface Display Platform , has resulted in significant improvements of antigen binding affinity.


Antibody affinity maturation library design based on computational design.


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Computer-Based Modeling predicts the key amino acid residues in the antibody–antigen interaction interface. The green band indicates the single chain antibody and the blue band indicates the N-terminal of the antigen. The yellow bar indicates key residues in the single-chain antibody, and the red band indicates key residues in the antigen. 


Affinity-improved mutation variants are obtained from yeast surface display platform.


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In order to optimize the binding affinity of an antibody, a 3D structure of an antibody–antigen complex was analyzed. Antibody affinity maturation library (Fab) was constructed based on computer modeling. By performing 3 rounds of FACS sorting, affinity improved clones with high expression (anti-Kappa-PE) and binding activity (APC-Ag) were isolated for the following functional validation.


In vitro validation.

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Mutations had achieved 20-200 fold improvement in affinity. 

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