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OMass is a world-leader in native mass spectrometry that allows protein targets to be studied in a folded native-like state thereby preserving any associated non-covalent interactions. This allows drug interactions to be captured as well as the influence of those drugs on downstream interaction networks that are necessary for dictating function. In this way, the technology delivers superior resolution to traditional pharmacology assays enabling a clearer, more detailed picture of how a putative ligand engages a protein target with function evaluated in parallel. The additional information obtained in the OMass assays can reveal new biology even at well-studied receptors and the cell-free system is unbiased for different ligand chemistries unmasking chemical space of high therapeutic potential inaccessible to cell-based assays.

The platform is based on work initiated by our scientific founders in the laboratory of Professor Carol Robinson at Oxford University and is currently being applied to G-protein coupled receptors and other membrane proteins where we have developed a portfolio of intellectual property protection. We are optimizing and automating our approach and this is part-funded by an Innovate Grant, awarded in March 2018.


We have initiated programs against three high impact G-protein coupled receptor targets (GPCRs) with a focus on genetically defined patient populations and/or immunological dysfunction. We are actively evaluating additional GPCRs and solute carriers aligned with our focus on immunology and genetic disease

Native Mass Spectrometry

Protein assemblies are introduced to the mass spectrometer, using nano-electrospray ionization. The technique allows very accurate mass measurement whilst maintaining their native conformations and interactions with drugs.

Preserving Structure

Non-covalent interactions are preserved and detected.

Structural Mass Spectrometer Analysis

The resulting spectra allows the equilibrium between each component and complex formation to be captured, directly reporting on stoichiometry and ligand binding.


A protein complex is introduced to a labelling solution, which labels solvent accessible areas of the assembly. Labelled areas of the complex can be identified due to the increase in mass induced by the label.


Regions involved in protein-protein interactions can be identified since they have a lower propensity to be labelled. This also enables identification of drug binding sites.

Screening with Native Mass Spectrometry

In a multi-well plate, the protein is incubated with a compound library. Using automated injection, each mixture is analysed by native mass spectrometry to check for binding.