Membrane proteins represent the largest class of therapeutic targets. They exhibit their biological function through dynamic structural modifications in response to voltage, pH, and binding to small molecules (ligands) or proteins they interact with. These dynamic molecular reorganizations occur out of equilibrium. Yet, our understanding of functional activities of membrane proteins is largely driven by static structural insights imposed by the constraints in traditional equilibrium systems.
NOVATARG has licenses to patented technologies demonstrating the company’s unique potential to enable structural and functional characterization of full-length cell-surface receptors and viral antigenic targets, in native, physiologically relevant conformational and oligomeric states.
Our approach is expected to overcome the drawbacks of traditional structural biology methods, including crystallization, single particle, cryo-EM and NMR, which often require:
In contrast, the images we have produced using our nonequilibrium imaging technology demonstrate an exceptionally high signal amplification attributed to the spontaneous alignment of millions of single particles in various orientations during the process.
We explore laser-enhanced fluorescence imaging, cryo-electron diffraction, and computational algorithms for rapid characterization of complex structural dynamics of membrane protein interactions in two distinct ranges of resolution. This involves exploration within the low to intermediate resolution range, suitable for functional screening applications, and the near-atomic to atomic resolution range, specifically applied for structure-based drug discovery.
Our experimental findings offer insights into promising avenues to streamline the characterization of distinct structural features of membrane protein dynamics, in native, functionally active, biologically relevant states, suitable for biomedical research and drug discovery advancements.
