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Our affinity maturation platform combines computational modeling, rational library design, mutagenesis strategies, and quantitative yeast display screening to efficiently identify affinity-enhanced antibody and nanobody variants.
Binding affinity is one of the most critical properties influencing the performance of therapeutic antibodies and nanobodies. Improved affinity can enhance target engagement, biological activity, sensitivity, and therapeutic efficacy.
However, affinity optimization must be carefully balanced with specificity, stability, expression, and developability. Excessive engineering may negatively affect antibody behavior and downstream manufacturability.
Our affinity maturation workflows combine computational modeling, rational mutagenesis strategies, and quantitative yeast display screening to efficiently identify affinity-enhanced antibody and nanobody variants while preserving developability characteristics.
Structure-Guided Library Design
Computational modeling and antibody-antigen interaction analysis are used to identify key interface residues and potential affinity-enhancing mutation hotspots. This approach improves screening efficiency while reducing unnecessary library complexity.
Quantitative Yeast Display Screening
Our yeast display platform enables precise FACS-based selection of high-affinity variants through quantitative analysis of binding and expression simultaneously. This workflow supports high-throughput variant screening and enrichment of rare high-affinity clones.

|
Service item |
Delivery |
Time |
|
Computer-Based Modeling |
Affinity-improved variant sequences Purified optimized antibodies Affinity and functional analysis results |
8-13 weeks |
|
Affinity maturation library construction and screening |
||
|
Candidate expression and validation |
Structure-Guided Affinity Maturation
Our proprietary computer modeling software is used to design targeted libraries for affinity optimization. As shown in Figure 1, this modeling predicts key interaction sites between the antibody and antigen. The resulting variant libraries are screened using our yeast surface display platform, yielding affinity-enhanced clones (Figures 2).

Figure 1. Computer Modeling of Antibody–Antigen Interaction.
Key binding residues at the interface were predicted through 3D structural modeling. Green: A yeast display affinity maturation library was generated based on computational hotspot analysis and screened through multiple rounds of FACS sorting.

Figure 2. Structure-Guided Antibody Optimization.
A yeast display affinity maturation library was generated based on computational hotspot analysis and screened through multiple rounds of FACS sorting.
In vitro Validation

Figure 3. Binding Affinity Improvement of Mutants Compared to Wild Type.
Selected mutants achieved approximately 20- to 200-fold affinity improvement compared with the parental antibody.