Antibody humanization is a necessary technology to mitigate potential immunogenic risks associated with animal-sourced antibodies, and it has been applied to the majority of therapeutic antibodies on the market. However, in the current context of antibody humanization, other characteristics must also be considered, including binding affinity, physicochemical stability, expression in host cells, pharmacokinetics and the fundamental approaches involved in antibody engineering.

（Hebditch M, et al. PeerJ. 2019）

Antibody humanization involves transplanting amino acids from the complementarity-determining region (CDR) onto human germline frameworks while retaining key non-human amino acid residues through back mutations. This is a delicate balance between introducing as many human sequences as possible to reduce the risk of immunogenicity while preserving the core amino acids of the parental antibody to maintain the original binding activity. Throughout this process, additional considerations are given to the developability of the antibody.

Our antibody humanization platform combines the advantages of rational and empirical antibody humanization methods. The humanization antibody platform is designed using our proprietary humanization and optimization algorithms, achieved through gene synthesis and fusion of humanized antibody variable regions with human antibody main chains.

After a comprehensive analysis of humanized parental monoclonal antibody sequences and structural information, multiple frameworks are selected from homologous human mature antibody germline sequences, avoiding potential limitations associated with specific frameworks in the design. 3D structure-based modeling is employed to identify positions in the humanized sequence requiring back mutations to restore CDR conformation and optimal antigen binding. Structural algorithms generate multiple possibilities for each position, determining the optimal antibody sequence to achieve the highest activity and specificity.