Abstract
Recombinant human follicle stimulating hormone (r-hFSH) is widely used for infertility treatment and is subject to the development of biosimilars. There are different purification strategies that can yield r-hFSH of pharmaceutical quality from Chinese hamster ovary cell culture broth. We developed a purification process for r-hFSH centered on immunoaffinity chromatography with single-domain recombinant camelid antibodies. The resulting downstream process is simple and devoid of ultrafiltration operations. Studies on chromatography resin resource and ligand leakage showed that the immunoaffinity matrix employed was suitable for industrial use and stable for at least 40 full chromatography cycles, and the leaked single-domain antibody ligand was completely removed by subsequent purification steps. All chromatography resins employed withstood the same 40 cycles of use without significant changes in separation efficiency and product binding capacity. The resulting industrial purification process yielded batches of r-hFSH with consistent levels of purity and bioactivity.
Highlights
Follicle-stimulating hormone (FSH) is a heterodimeric glycoprotein of the gonadotropin family, consisting of two non-covalently associated subunits
In the case of FSH and the corresponding immunoaffinity resin, we found it to be suitable for the laboratory-scale purification process of FSH [23], but no data have been published to date on resin stability, practical dynamic binding capacity (DBC), and ligand leakage dynamics in repetitive use cycles
We present the results of process studies for the FSH biosimilar drug, manufactured by a significantly simplified downstream process devoid of tangential flow filtration operations
Summary
Follicle-stimulating hormone (FSH) is a heterodimeric glycoprotein of the gonadotropin family, consisting of two non-covalently associated subunits (chains). The immunoaffinity purification of FSH enables the removal of both host cell-derived impurities and free FSH chains in one step; the overall downstream process may be simplified to five column chromatography steps and two viral inactiva tion steps. This process, as partially described in [23], consists of an initial ofsolvent/detergent viral inactivation step, performed on the clarified culture broth, multimodal, immunoaffinity, desalting by size exclusion, tandem ion exchange, and final size be simplified to five column chromatography steps and two viral inactivation. Materials and Methods of a pharmaceutical product with high biological activity and batch-to-batch consistency
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