Characterization of Disulfide Bonds in Bevacizumab Biosimilar Using A Q-TOF Mass Spectrometer

mAb biosimilars are emerging as the fastest-growing sector of biotherapeutics in the global pharmaceutical industry. To obtain the highest quality, mAb biosimilars need to be extensively and comprehensively characterized, as any differences between biosimilars and mAbs can significantly affect the efficacy and safety. Notably, disulfide bonds formed between cysteine residues are critical to protein folding and structural stability (incorrect disulfide linkages can cause a loss of biological activity or even can elicit an immune response from the host), and thus, the number of disulfide bonds and their positions should be monitored and controlled. In the present study, we applied a LCMS-based approach to precisely characterize disulfide bonds in bevacizumab biosimilar by a comparative analysis of reduced and non-reduced conditions.

Content Type:
Document Number:
ASMS 2020 - ThP 464
Product Type:
Liquid Chromatography Mass Spectrometry
Pharma & Biopharma, LCMS-9030 Q-TOF Mass Spectrometer
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