Investigating the Conformational Structure and Potential Site Interactions of SOD Inhibitors on Ec-SOD in Marine Mud Crab Scylla serrata : A Molecular Modeling Approach

AbstractSuperoxide dismutases (SODs) act as a first line of the enzymatic antioxidant defense system to control cellular superoxide anion toxicity. Previously, several inhibitors have been widely identified and catalogued for inhibition of SOD activity; however, still the information about the mechanism of interaction and points toward the inhibitor interactions in structures of SODs in general and in extracellular (Ec)-SOD in particular is still in naive. In the present research, we present an insight to elucidate the molecular basis of interactions of SOD inhibitors with Ec-SOD in mud crabScylla serrata using molecular modeling and docking approaches. Different inhibitors of SOD such as hydrogen peroxide\((\hbox {H}_{2}\hbox {O}_{2})\), potassium cyanide, sodium dodecyl sulfate (SDS),\(\beta\)-mercaptoethanol and dithiocarbamate were screened to understand the potential sites that may act as sites for cleavage or blocking in the protein. SOD –SDS and\(\hbox {SOD}{-}\hbox {H}_{2}\hbox {O}_{2}\) complex interactions indicate residues Pro72 and Asp102 of the predicted crab Ec-SOD as common targets. The GOLD result indicates that Pro72, Asp102 and Thr103 are commonly acting as the site of interaction in Ec-SOD ofS. serrata with SOD inhibitors. For the first time, the results of this study provide an insight into the structural properties of Ec-SOD ofS. serrata and define the possible involvements between the amino acids present in its active sites, i.e., in the regions from 7...
Source: Interdisciplinary Sciences, Computational Life Sciences - Category: Bioinformatics Source Type: research