Life is Interaction
We preserve the fidelity of the native target ecosystem outside the confounding complexity of the cell to precisely interrogate the fundamental interactions that drive life.
In cell-based systems, researchers know that biology is observed with high fidelity. However, there is a disconnect between what is measured and the drug’s action resulting in false leads and missed opportunities.
In cell-free approaches, confounding factors have been stripped away giving precise data on how tightly or how quickly a drug binds to its target. However, the target protein no longer faithfully represents its living counterpart and endogenous biomolecules are absent.
OMass’ platform advantages
OMass’ platform retains biological relevance at high resolution, delivering cell-system fidelity with cell-free precision.
- Faithful to the native ecosystem. We use proprietary biochemistry to preserve downstream partners, lipid interactions and endogenous regulatory molecules.
- Biology distilled to its essential elements. We use our patent protected native mass spectrometry (MS) technology to measure the physical interactions that drive biology.
- The full spectrum of pharmacology. We leverage custom chemistry enabled for MS to interrogate binding and multiple discrete biological outcomes rationally and systematically.
Combining the biological richness of a cell-based assay with the precision of a cell-free method allows us to go after the best targets. We can:
- Unambiguously link binding and function driving smart lead optimization and avoiding blind alleys from indirect effects
- Capture a broad range of affinities identifying low affinity starting points at challenging targets that are lost in other assays through our combination of native, precise measurements
- Unlock novel biology by identifying binders without the filter of an activity threshold; important for targets driving more than one biologically relevant outcome
- Identify natural allosteric sites from endogenous regulatory molecules and exploit these for drug discovery, critical when the orthosteric site is intractable to small molecules