Herbs are essential resources for drug discovery. However, numerous challenges stand in front of the scientific community to discover novel drugs from herbs. To explore the validation behind the precious knowledge of traditional medicine, we focused on achieving virtual screening to detect the potential medicines from the herbs.  Five bioactive compounds from known anti-inflammatory medicinal plants were examined through molecular docking against  cyclooxygenase-2 (COX-2) and inducible Nitric Oxide Synthase (iNOS), using AutoDock 4.2. The docking of selected ligands with COX-2 showed the binding energy varying from -6.15 Kcal/mol to ‑11.24 Kcal/mol. The docking energies of identified ligands with iNOS were generated ranges from -3.85kcal/mol to -6.99 kcal/mol.  Among the tested ligands, it was noted that 6 urs-12-en-24-oic acid showed the best binding energy than other compounds with the lowest binding energy and highest binding affinity with both anti-inflammatory target proteins COX-2 and iNOS. The in silico study validates the potential phytochemical compound of the medicinal herb that contribute to anti-inflammatory activity with low toxicity and minimal side effects.

Thamaraiselvi et al.: In Silico Molecular Docking on Bioactive Compounds against Type 2 Diabetic Target ProteinsNatural chemical compounds from medicinal plants used for the healing of diseases and disorders with fewer side effects, easy accessibility and economically cheap. The current study was aimed at finding novel drug like molecules as anti-diabetic compounds using in silico approach. Intermolecular interactions between target proteins and different antidiabetic compounds were observed. Five phytocompounds were selected from Plumbago zeylanica, Neolitsea cassia and Wrightia tinctoria and taken for molecular docking against human pancreatic alpha-amylase and human dipeptidyl peptidase IV using Autodock 4.2. Among the five phyto compounds, 6 urs-12-en-24-oic acid Plumbago zeylanica is the best compound for both the human pancreatic alpha-amylase and human dipeptidyl peptidase IV inhibition, as it possessed higher value in molecular dockings.