下游加工
上游和下游(DNA)
单克隆抗体
下游(制造业)
重组DNA
化学
中国仓鼠卵巢细胞
计算生物学
上游(联网)
靶蛋白
抗体
色谱法
酵母
细胞生物学
生物化学
细胞
热休克蛋白
热休克蛋白70
细胞培养
过程开发
蛋白质工程
生物
蛋白质A
子类
人类蛋白质
药物开发
蛋白质纯化
分子生物学
同源(生物学)
药品
亲和层析
作者
Greg Evangelist,Chris Kwiatkowski,Krishnakumar Malu,Suli Lu,Linda Yi,Sarwat F. Khattak,Brad Stanley
摘要
Host cell proteins (HCPs) are critical process-related impurities of recombinant protein biopharmaceuticals that have the potential to impact product safety and efficacy. In this study, two residual HCPs, heat shock protein 90 beta and perilipin-4-like, produced from a CHO cell line, were identified during the development of a late-stage platform Immunoglobulin G subclass 1 (IgG1) monoclonal antibody process. A risk assessment was performed that included identification of HCPs, homology with their human protein counterparts, and prior non-clinical and clinical experience. The outcome deemed these two species as "problematic" and target levels were established to guide approaches for removal. Given the high productivity of the upstream and downstream platform processes, the goal was to explore conditions that minimize deviations from the platform. An end-to-end approach was performed that evaluated downstream levers, including Protein A washes, polishing chromatography operational parameters, and exploration of depth filter media. Upstream levers were also explored, evaluating effects of temperature shift and modulation of iron and citrate to help control levels of both HCP species. The results presented in this study demonstrated the upstream and downstream conditions achieved effective removal of the two HCP species to meet drug substance targets.
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