@article {2175, title = {In silico ADME and Drug-likeness Evaluation of Phytochemicals from the Leaves of Tabernaemontana divaricata Linn.}, journal = {Pharmacognosy Journal}, volume = {15}, year = {2023}, month = {December 2023}, pages = {1136-1142}, type = {Research Article}, chapter = {1136}, abstract = {

Introduction: Tabernaemontana divaricata is a traditional plant from the family of Apocynaceae, which has wider medicinal activities such brain tonic, anti-epileptic, anti-mania and anti-oxidant. The current predictive study was aimed to know pharmacokinetics and drug likeness of selected phytochemicals present in T.divaricata by using online tool Swiss-ADME. Methods: The air-dried leaves were pulverized and subjected to Soxhlet extraction and percolation using the solvents, namely, ethanol, hydroalcoholic solvent (50:50 and 70:30 ethanol: water) and water to obtain four different extracts. Aqueous extract was made through percolation. Subsequently, gas chromatography-mass spectrometry was used to analyze each extract further. All the bioactive compounds were subjected to in silico ADME and drug-likeness studies and the finalized compounds were undergone cell cytotoxicity activity. Results: All the four extracts have distinct physicochemical properties linked to the chemicals naturally present in large amounts in T. divaricata leaves. The compound 4,4,7a-Trimethylhexahydro-1-benzofuran-2(3H)- one and 2-(4-methylphenyl) indolizine having good drug likeness of 4.50 and 3.50 respectively and good lipophilicity which has the log P value of 2.51 and 3.73 appropriately. IC50 values of compounds were found to be 312.1 {\textpm} 0.2μg/ml for 4,4,7a-Trimethylhexahydro-1-benzofuran-2(3H)-one and 393.7 {\textpm} 0.2μg/ ml for 2-(4-methylphenyl) indolizine. Conclusion: Major bioactive chemicals were found in the aqueous extract and based on the calculated ADME parameters they are anticipated to serve as cytotoxic lead compounds. It is advocated that current predictive results should be authenticated by in vitro and in vivo toxicological and pharmacological assay.

}, keywords = {Apocyanceae, Cell cytotoxicity studies, GC-MS analysis, In silico study}, doi = {10.5530/pj.2023.15.207}, author = {Ayda Cherian and Velmurugan Vadivel} } @article {1914, title = {An In Silico Study to Explore the Role of EGFR in Ovarian Cancer}, journal = {Pharmacognosy Journal}, volume = {14}, year = {2022}, month = {December 2022}, pages = {817-821}, type = {Research Article }, chapter = {817}, abstract = {

EGFR is a tyrosine kinase receptor that has a role in the tumorigenesis of many types of solid tumors. Aberrantly phosphorylated or overexpressed EGFR is associated with cellular proliferation, prevention of apoptosis, activation of invasion and metastasis, and stimulation of tumor-induced neovascularization. EGFR{\textquoteright}s hyperactivity has been observed in ovarian cancer. Although conventional chemotherapy and surgery for advanced ovarian cancer have improved over the years, still there is a critical need for the development of molecular targeted therapies. The major challenge for this approach is the complete understanding of the protein structure of this mega receptor. In this study, we explored this receptor using in silico tools. The protein structure of the EGFR kinase domain (PDB ID: 1M17) and co-crystal containing EGFR and PTP1B kinase domain fragment (PDB ID: 3I7Z) were obtained from the RCSB Protein Data Bank. We performed protein-protein docking using BioLuminate. It was found in this study that the DADEYL segment of EGFR (position 988-993) which includes autophosphorylated tyrosine at position 992, is the segment that is responsible for the overexpression of this receptor in ovarian cancer. There are currently two main classes of clinically-approved drugs which downregulate EGFR activity; tyrosine kinase inhibitors (TKIs) and monoclonal antibodies (Mabs). However, treatment with both type of therapies has been met with shortcomings. Therefore, there is a need for further studies to explore the suitable ligands that can downregulate its activity.

}, keywords = {EGFR, In silico study, Protein-protein docking, Tyrosine kinases}, doi = {10.5530/pj.2022.14.173}, author = {Vikash Jakhmola and Tarun Parashar and Pallavi Ghildiyal and ANM Ansori and Rajeev Kumar Sharma and N. G. Raghavendra Rao and Kapil Kalra and Nishan Singh and Nidhi Nainwal and Rajeev Kumar Singh and M. P Singh and Vishwadeepak Kimothi and Alok Bhatt and Ashish Dimri and Ravi Kumar and Amit Semwal and Nur Sofiatul Aini and Maksim Rebezov} }