flare
Streamline new molecule design
Electrostatic Complementarity™ (EC) scores and maps provide rapid activity prediction with visual feedback on new molecule designs, and prove invaluable for understanding ligand binding, structure-activity relationships and for ranking new molecule designs.
Flare™ uses the XED force field to calculate a detailed map of the electrostatic character of the protein active site and your ligand. The interaction potentials provide you with vital knowledge of the fundamental processes that underlie ligand-protein binding, helping you to perfect the design of new molecules.
- Reveal the electrostatics of the active site
- Compare electrostatic patterns across a protein family to design more selective ligands
- Design new molecules with the ideal electrostatic properties to bind strongly to your protein
- Gain vital insights into your SAR by comparing the electrostatics of multiple ligands
- Electrostatic Complementarity as a Fast and Effective Tool to Optimize Binding and Selectivity of Protein–Ligand Complexes J. Med. Chem. 2019, 62, 6, 3036-3050
Electrostatic Complementarity maps
PDB entry 4UIV illustrating areas where protein-ligand electrostatics are favorable (green) and where electrostatics could be improved (red).
Protein interaction potentials
Full protein interaction potential maps guide the placement of ligand atoms.
Quick and easy visual assessment of electrostatic trends
Interaction fields can be mapped onto protein surfaces allowing quick and easy visual assessment of electrostatic trends across protein families.
Immediate feedback on electrostatic changes
Designing new ligands in Flare gives you immediate feedback on electrostatic changes while viewing your molecule in the protein active site.
Flare
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