Catherine Pemberton-Ross | Principal Scientist II
Novartis
Dr Catherine Pemberton-Ross is a Principal Scientist at Novartis in Basel, Switzerland, specialising in bioanalysis for biologics and novel large-molecule therapeutic modalities. She holds a PhD in Biochemistry from the University of Cambridge, UK, and has more than 14 years of experience in the biopharmaceutical industry. Throughout her career, she has worked across target identification and validation, drug discovery, preclinical development and early clinical programmes for biologic therapeutics, providing a broad perspective on the challenges associated with translating scientific discoveries into medicines and advancing them toward the clinic. Her current work focuses on developing bioanalytical strategies to support biologic therapeutics from preclinical research through early clinical development. She is particularly interested in the evolving challenges of large-molecule bioanalysis, immunogenicity assessment and translational approaches that support the development of innovative medicines.
Appearances:
Festival of Biologics Day 2 @ 16:50
Protein Quality as a Critical Factor in Target Interference Assessment for Bioanalytical Assays
Assessment of target interference is a critical aspect of immunogenicity assay development for complex biologics, particularly when soluble endogenous ligands may affect anti-drug antibody (ADA) detection. A key requirement for reliable assessment is the selection of a recombinant protein that closely represents the endogenous ligand; however, identifying a suitable surrogate can be challenging.
During development of a bridging ADA assay for a biological therapeutic targeting a soluble protein, significant target interference was observed. This prompted further investigation into the properties of the recombinant protein used for the interference assessment.
Here, we present a detailed analytical comparison of recombinant target proteins obtained from multiple suppliers. Substantial differences in reagent attributes were identified, with several preparations showing characteristics unlikely to reflect the native endogenous protein. From this assessment, a high-quality recombinant protein equivalent to the endogenous form was identified, which eliminated the observed target interference in the assay.
These findings demonstrate that impurities and non-native protein conformations in recombinant target reagents can lead to misrepresentation of target interference in bioanalytical assays. Careful selection and characterisation of critical reagents are therefore essential to ensure accurate, clinically relevant immunogenicity assessments and the development of robust ADA assays.
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