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1 Introduction Proteins are fundamental biomolecules with a wide variety of structural and functional variations, driving virtually all biological processes, from acting as enzymes and structural components to facilitating signaling and transport [1, 2]. Advances in biotechnology have enabled the recombinant production of proteins, allowing their broad application across various fields, most notably in the development of biopharmaceuticals [3, 4].
Introduction Click to copy section linkSection link copied! Monoclonal antibodies (mAbs) typically contain N-linked oligosaccharides (N-glycans) attached to the Fc region of the heavy chain. Modifications in their glycosylation profiles can impact their pharmacokinetics and protein efficacy. (1) Thus, determining the glycoform profile of therapeutic mAbs is essential.
Introduction Click to copy section linkSection link copied! Native mass spectrometry (nMS) is increasingly applied in structural and molecular biology to analyze intact proteins, protein-small molecule interactions, and noncovalent complexes. (1−3) With nMS, protein assemblies can be retained in the gas phase to get insights into their molecular composition and high-order structure.
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