Greenlight Biosciences

 

The problem biosimilar antibody makers have to solve is matching the properties of the original drug. During manufacturing, antibodies are produced in cells that attach various sugar structures like fucose. The FDA and EMA have indicated that biosimilar antibody manufacturers should compare receptor binding of their candidate to that of the innovator drug. Biosimilar drugs with equal nonfucosylation levels as those of the innovator drugs would have similar receptor binding and therefore be likely to gain regulatory approval.

Zepteon has developed Glycap-3A, a unique, breakthrough, patent pending (WO2013013193 and US 20130084648 A1) affinity purification technology that addresses this critical need for biosimilars makers by enabling separation of antibodies based on their fucose levels. The affinity purification resin contains optimally immobilized FcgammaR3A receptors, leading to an antibody equilibrium binding capacity above 8 mg/ml. The percentages of nonfucosylated antibodies have been highly enriched using these resins, as shown below

Bolton et. al, Biotech Prog, April 2013; btpr.1717

Pace et. al, Biotech Prog, June 2016; btpr.2300

glycan

Zepteonís Glycap-3A resin can be used to make a biosimilar antibody with a nonfucose level that matches that of the original drug, or one with a nonfucose level at the upper end of the range of the original drug for use in structure function studies (Pace et. al, Biotech Prog, June 2016; btpr.2300). The economical, fast and robust Zepteon separation method is superior to cellular methods of targeting fucose levels. Cellular methods like genetically engineering cells or screening cell lines and bioreactor conditions are slow, complex and costly.