Hydrogen/Deuterium Exchange Mass Spectrometry of Proteins and Biosimilar Drugs
This research develops and applies hydrogen/deuterium exchange mass spectrometry (HDX-MS) for determining the dynamics and physical-chemical properties of proteins, biopharmaceuticals, glycoproteins, peptides, peptide-metal complexes, receptors, and biocatalysts. Topics of particular interest include the effects of post-translational modifications (PTMs) on protein dynamic structure and protein-ligand interactions, structure-function relationships between glycan structure and glycoprotein folding, and comparability measurements among innovator drugs and biosimilar drug candidates. The HDX-MS laboratory can now conduct measurements on membrane and transmembrane proteins with fully automated apparatus. Research is conducted at the nearby NIST & UMD joint Institute for Bioscience & Biotechnology Research. The well-equipped laboratory includes a fully automated HDX Orbitrap tandem mass spectrometer with ETD capability, a cryo-EM, SAXS, neutron source, a wide variety of analytical and preparation chromatographs, and numerous optical/NMR spectroscopic instruments.
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