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• W2023606304 abstract "Robust higher order structure (HOS) characterization capability and strategy are critical throughout biopharmaceutical development from initial candidate selection and formulation screening to process optimization and manufacturing. This case study describes the utility of several orthogonal HOS methods as investigational tools during purification process development. An atypically high level of residual detergent in a development drug substance batch of a therapeutic monoclonal antibody triggered a root cause investigation. Several orthogonal biophysical techniques were used to uncover and characterize a specific interaction between the detergent and the antibody. Isothermal titration calorimetry (ITC) was used to quantify the molar ratio and affinity of the binding event, and circular dichroism (CD) spectroscopy and differential scanning calorimetry (DSC) were used to evaluate corresponding impacts on secondary/tertiary structure and thermal stability, respectively. As detergents are used routinely in biopharmaceutical processing, this case study highlights the value and power of HOS data in informing technical investigations and underlines the importance of HOS characterization as a component of overall biopharmaceutical analytical control strategy." @default.
• W2023606304 created "2016-06-24" @default.
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• W2023606304 date "2015-04-01" @default.
• W2023606304 modified "2023-09-25" @default.
• W2023606304 title "Technical Decision-Making with Higher Order Structure Data: Specific Binding of a Nonionic Detergent Perturbs Higher Order Structure of a Therapeutic Monoclonal Antibody" @default.
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• W2023606304 doi "https://doi.org/10.1002/jps.24293" @default.
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