Macro molecular X-ray Diffraction (XRD), 600 MHz NMR and Computational Chemistry are employed to characterize the 3-dimensional structures of Proteins and Protein-ligand complexes. Multidimensional NMR, in conjunction with isotope labeling is used to characterize binding sites in the solution phase.

Aurigene has successfully solved more than 40 structures in house, belonging to diverse protein classes, many of them novel using XRD over last two years. Aurigene has crystallography access to synchrotron beam time at multiple facilities, including ESRF Grenoble, France and Brookhaven National Laboratory, USA for higher resolution structural studies.

Aurigene leverages its expertise in NMR to identify weakly-binding ligands. Dissociation constants of Protein-ligand complexes are determined by Pulsed-field gradient NMR (PFG-NMR) through the measurement of translational diffusion coefficients.

NMR is used extensively for binding-site characterizations, solving the conformations of ligands in the receptor-bound state, NMR-based assays and Diffusion coefficient measurements.

Hit generation and Lead optimization efforts are highly focused and supported by Computational Chemistry efforts involving virtual screening, pharmacophore modeling, molecular docking, homology modeling, QSAR and In-silico ADME properties prediction.

Fragment based approach is utilized by Aurigene to identify novel hits which can be further optimized. To this end, Aurigene has carefully compiled a collection of small molecule fragments which are screened using ligand based NMR or Crystallography methods.

The fragment library is comprised of general drug like fragments (ca. 200) & target specific compounds for kinases, proteases & NHRs (ca. 100 each). In addition, we have a unique set of about 50 natural product fragments of key pharmacophore moieties from bioactive natural products.