Eriodictyol Eriodictyol was suggested by Smith and Smith as an interfatial inhibitor between the virus S-protein and human ACE2 receptor . Eriodictyol's conformations are predominately determined by a rotatable bond that connects the two ring systems, and by the envelope conformations adopted by the 4-chromanone residue. These envelope conformations result in either an overall bent structure (e.g. conformer 1, ∆E=0.000 kcal•mol -1 ) or a more linear structure (e.g. conformer 2, ∆E=0.035 kcal•mol -1 ; Figure ). The final factor that determines the conformations are the hydroxyl orientiations. A total of 49 stationary points were identified at the B97-D3(BJ)/cc-pVTZ theory level, with 16 minima being below a relative energy of 1.2 kcal•mol -1 (Tables ).