Analysis of Monoclonal Antibodies and Antibody Drug Conjugates (ADCs) / MALDI & Q-TOF

Applications for MALDI & Q-TOF


Analysis of Glycopeptides of Monoclonal Antibody Using MALDI-7090 High-Resolution MALDI-TOF MS

Antibodies that are utilized in biopharmaceuticals are often subjected to glycan modification. This glycan is a molecule with high structural heterogeneity consisting of intricately coupled monosaccharides, such as glucose and mannose, and that complex structure is known to play an important role in the functional regulation of proteins. However, information such as the complex structure of the glycan and the site at which the glycan is attached to the protein is not written into the gene beforehand. Rather, it is information that is formed based on the actions of many glycosyltransferases during the process of protein biosynthesis.


Simplified Mass Measurement of Chemically-Modified Antibodies: Determination of the Presence of the Number of Modifications Using a Linear Benchtop MALDI-TOF MS

Antibody drug conjugates (ADC), a type of pharmaceutical composed of an antibody bound to a drug, appeared in the 2000s with the expectation they would serve as more effective anti-cancer drugs than previous small-molecule pharmaceuticals through the combination of the antibody's high selectivity and the availability of a smallmolecule drug. With a small number of products already available in the marketplace, the degree to which and where binding occurs are important characteristics to determine quality when compounds are artificially bound to proteins, as in the case of ADCs.


Analysis of Modification Site of Chemically Modified Antibody Using MALDImini-1 Compact MALDI Digital Ion Trap Mass Spectrometer

Antibody drug conjugates (ADC), which appeared in the 2000s, are a new class of anti-cancer drugs in which an antibody is bound to a cytotoxic drug. Because they combine the high substrate specificity of the antibody and the effect of a lowmolecular drug, ADC are expected to be more effective anticancer drugs than the conventional low-molecular drugs. When a different compound is bound artificially to a protein, as in the case of ADC, the binding degree of that compound and its binding site become one of the critical quality properties.


Disulfide Bond Characterization of Monoclonal Antibody Using Q-TOF Mass Spectrometer

Monoclonal antibody is emerging as the fastest growing category of biotherapeutics with a wide range of therapeutic and diagnostic applications. Higher-order structure of mAb plays a critical role in the efficacy and safety. For example, the number of disulfide bonds and their positions are critical attributes (CQAs) for mAb, because incorrect disulfide linkage formation can cause a loss of biological activity or even can elicit an immune response from the host. Herein, we report a LCMS based method to precisely characterize disulfide bonds in mAb biosimilar by comparative analysis of non-reduced and reduced conditions.

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