Publications

Host cell protein (HCP) characterization in monoclonal antibody (mAb) products is challenged by a large concentration gap between low-abundance HCPs and high-abundance mAb proteins. Advances in sample preparation, chromatography, and mass spectrometry techniques have aimed at either reducing this concentration imbalance or the peptide coelution effects during chromatography. Despite this, comprehensive characterization of HCPs remains difficult, particularly at below-ppm levels, often requiring...

Fluorescent capillary gel electrophoresis (CGE) with sodium dodecyl sulfate (CE-SDS) provides a powerful, high-sensitivity alternative to ultraviolet (UV)-based detection for characterizing therapeutic monoclonal antibodies (mAbs). Regulatory and standards organizations, such as the United States Pharmacopeia (USP), include only UV-based CE-SDS methods, hindering the adoption of alternative detection methods. There is growing opportunity to expand beyond exclusively UV-based CE-SDS methods. In...

Disulphide bonds contribute to the conformational structure of monoclonal antibodies (mAbs) and are therefore vital for their stability, biological function and safety. However, the biopharmaceutical manufacturing process can influence these bonds, potentially leading to the formation of free thiols, scrambled configurations, or degradation products, which may negatively impact quality and safety. Current analytical strategies for characterising disulphide bonds and free thiols in mAbs are...

Characterizing post-translational modifications (PTMs) in monoclonal antibody products is critical for ensuring product quality attributes understanding and monitoring. While the bottom-up approach is widely adopted, it suffers from the loss of molecular connectivity and is susceptible to artifact generation. Conversely, top-down approaches face limitations due to the high complexity and poor gas-phase fragmentation of large intact molecules to get site-specific post-translational information...

The end-to-end characterization of a fed-batch bioprocess for expressing a non-originator version of the NISTmAb IgG1 (cNISTmAb) using NISTCHO, a high-performance CHO production cell line available as a NIST reference material (RM 8675), is described. NISTCHO was developed to support bioprocess reproducibility, cross-laboratory standardization, technology benchmarking, and collaborative innovation in biomanufacturing process research. Propagation, scale-up, and cultivation of NISTCHO in...