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
- File Name:
- File Size:
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