In Silico Estrogen Receptor Activity Evaluation of Some β-Carboline Derivatives Through Molecular Docking Approach and Target Prediction by ADME Study

A series of β-carboline derivatives have been modified at c-1 sites of the aryl ring and tested for the insilco estrogen receptor inhibitary study. all of the designed molecules show the excellent bonding score with 5acc estrogen receptor protein. the position of proposed ligand bc-6, bc-12 in the binding site of protein is superimposable with the native ligand and indicates the hydrogen bonding with the leu: 346 amino acid residues. the adme studies reveal that groups bc-6 and bc-12 show good human intestinal cyp1a2 inhibitor, cyp2c19 inhibitor, cyp2c9 inhibitor, cyp3a4 inhibitor, and cyp3a4 inhibitor activity with log kp (skin permeation)-5.43 cm/s, while ramachandran plot for bc-6 indicate, molecules shows the 100% favourable region in the pocket of enzyme 5acc, while the bc-6 and bc-12 can cross the bbb barrier. this study indicates that from all the synthesized molecules, the scaffolds bc-6 and bc-12 illustrate the excellent activity.