Our extensive track record in mass spectrometry over the last 20 years includes complex studies for proteins, biologics, nucleic acids, lipids and sugars either for protein characterization, hit binding studies or screening.
Native mass spectrometry is a fast and reliable technique which can provide both qualitative and quantitative information: affinities, and orthosteric/allosteric binding site assessment. Online SEC-UV-nMS allows rapid measurement of protein complexes as well as PROTAC recruitment, molecular glue or destabilizing compounds.
We offer deep expertise in the structural characterization of monoclonal antibodies (mAbs) and their derivatives applying top-down, middle-down and bottom-up strategies. Epitope and paratope binding sites are accurately mapped using hydrogen–deuterium exchange mass spectrometry (HDX-MS).
Our MS team is highly experienced in covalent screening (2D-LC MS) workflows, from compound management to binding site identification and kinetic measurements (kinact/Ki), even in large protein complexes.
Additionally, we provide robust non-covalent screening and binding validation using Affinity Selection Mass Spectrometry (ASMS, 2D-LC), enabling confident hit identification and interaction profiling.
| Screening | Binding | Target characterization | Biologics and biosimilars |
| • Covalent • ASMS: non-covalent | • Affinity, Stoichiometry • PROTAC recruitement • Allosteric and orthosteric ligands • Binding site mapping (covalent and non-covalent) • Protein dynamics by HDX-MS | • Protein / Protein complex QCs (denaturing and native MS) • Intact mass • Membrane protein (HDX-MS) • PTMs quantifications • Detection of fortuitous ligands | • Characterization (top, middle, bottom up) • Epitope / paratope mapping • mAb / Ag binding measurement • DAR quantification (ADC) |
Novalix has published a breakthrough study in Scientific Reports on GPBAR1, a GPCR linked to metabolism and inflammation. Using cryo-EM, HDX-MS, and mass photometry, we uncovered the molecular dynamics of GPBAR1-Gs interactions—advancing therapeutic targeting of metabolic disorders:
• 76.4% sequence coverage,
enabling reliable comparison
between apo GPBAR1 and the
ligand-bound GPBAR1/Gs complex.
• Revealed the dynamic
conformational changes that
occur during complex assembly
and activation.
• Findings align with cryo-EM data
Fig 1. Differential HDX-MS data (between apo GPBAR1 and GPBAR1/Gs complex) are mapped on cryo-EM structure. Protected peptides are in red.
Leverage our mass spectrometry expertise to drive deeper insights and enhance your discovery efforts.
Discover the benefits of mass spectrometry in the dedicated chapter of the book by Jean-Paul Renaud—cofounder and President & Chief Scientific Officer at Urania Therapeutics, and also cofounder of Novalix.
Structural Biology in Drug Discovery: Methods, Techniques, and Practices.
Drive your discovery forward with advanced mass spectrometry — contact us to discuss your project.