Molecular docking and molecular dynamics simulation studies on PLCE1 encoded protein

Abstract

Phospholipase C epsilon gene (PLCE1) is encoded the 1-phosphatidylinositol 4,5- bisphosphate phosphodiesterase ɛ-1 protein. This protein is characterized by the fetal onset of enormous proteinuria following by severe steroid resistance nephrotic syndrome (SRNS). The mutation position is located on the PIPLC_X domain of PLCE1 encoded protein. Molecular docking study was carried out between aegeline, berberine, diterpenoid, roseoside phytochemicals with wild type and mutant of the PIPLC_X domain of the PLCE1 gene encoded protein. From the molecular docking study, it was found that, due to mutation the binding energy was decreased for aegeline, berberine diterpenoid and roseoside with mutant PLCE1 at S1484L compared to wildtype. To achieve the depth analysis, we extended our study by performing the molecular dynamic simulation of 100 ns on wild type and the mutant (S1484L) model of above said domain of the studied protein. In the MD simulation study, we analyzed the result obtained from root mean square deviation, root mean square fluctuation, radius of gyration, salvation accessible surface area, hydrogen bond number and principal component analysis. These dynamical behaviour results of wild type protein show similar behaviour with mutant protein.