Process Development for Fc-Fusion Proteins
Since the first description in 1989 of a CD4-Fc fusion protein, interest in this class of engineered proteins has grown. Fc-fusion proteins are bioengineered polypeptides that join the crystallizable fragment (Fc) domain of an antibody with another biologically active protein domain or peptide to generate a molecule with unique structure-function properties and significant therapeutic potential. Fc-fusion proteins have numerous biological and pharmaceutical applications, which has launched Fc-fusion proteins into the forefront of drug development.
Fig. 1 Construction of an Fc-fusion protein.
With advanced technology and experienced staff, Creative Bioarray provides cell support services in the process development for Fc-fusion proteins to help our customers worldwide. We delivered rapid and accurate results to assist customers to accelerate their research.
Our Processing of Fc-Fusion Proteins
- Molecule design. When designing fusion proteins, the first step is to choose the individual module orientation, which can have a huge impact on function and production. Another important element is the linker joining both fragments. Furthermore, the length of the peptide spacer is a variable of interest. Finally, the design of a cleavable linker for fusion proteins needs to be considered.
- Upstream processing. After defining the molecular design of the protein, it needs to be expressed in production cell lines. The type of the heterologous fusion protein can have a strong influence on the selection of the host organism. In most cases， Chinese hamster ovary (CHO) cells are the host of choice as significant knowledge exists about their physiology and in vitro cultivation which was acquired over a long time.
- Downstream processing. Purification of Fc fusion proteins from expression systems typically involves harvest by centrifugation and/or filtration to yield a clarified supernatant. Each subsequent purification step is chosen based on a given fusion protein's structural characteristics to remove additional protein and nonprotein impurities.
The Role of Cell Banks in Fc-Fusion Proteins Manufacturing
- Providing expression systems to produce Fc-fusion proteins. Structurally complex Fc-fusion glycoproteins are mostly produced by mammalian expression systems. They require complex posttranslational modifications, such as glycosylation, γ-carboxylation, sulfation, and intra- and interchain disulfide-bonded domains, to maintain their structure and function.
- CHO cells are the most popular cell line for the expression of Fc-fusion proteins because they adapt well to serum-free culture, offer high-titer expression, and facilitate scale-up. Our cGMP-compliant CHO cell banking service is capable of providing strong support for the Fc-fusion proteins process.
- Human embryonic kidney 293 (HEK293) cells are another choice for the expression of Fc-fusion proteins due to their particular posttranslational processing requirement (γ-carboxylation). We provide sufficient material supply in the process development for Fc-fusion proteins by our cGMP-compliant HEK293 cell banking service.
- In fact, other cell lines such as mouse myeloma (NS0 or SP2/0) cells and monkey kidney (VERO) cells also have been used for Fc fusion proteins. We provide a uniform and intact cell population in the process of development for Fc-fusion proteins with our high-quality cell banking services.
As a professional services provider in the field of cell science, Creative Bioarray provides strong cell support in the process development for Fc-fusion proteins to our customers worldwide. We provide our clients with direct access to our experts and prompt responses to their questions. If you are interested in our services or have any questions, please feel free to contact us or make an online inquiry.
