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Starting from the lead structure we have identified in our previous works, weare extending our insight understanding of its potential inhibitory effectagainst both EGFR and HER2 receptors. Herein and using extended moleculardynamic simulations and different scoring techniques, we are providingplausible explanations for the observed inhibitory effect. Also, we arecomparing the binding mechanism in addition to the dynamics of binding with twoother approved inhibitors against EGFR (Lapatinib) and HER2 (SYR). Based onthis information, we are also designing and in silico screening new potentialinhibitors sharing the same scaffold of the lead structure. We have chosen thebest scoring inhibitor for additional in silico investigation against both thewild-type and T790M mutant strain of EGFR. It seems that certain substitutionpattern guarantees the binding to the conserved water molecule commonlyobserved with kinase crystal structures. Also, the new inhibitors seem to forma stable interaction with the mutant strain as a direct consequence of theirenhanced ability to form additional interactions with binding site residues.

In Silico Design, Extended Molecular Dynamic Simulations and Binding  Energy Calculations for a New Series of Dually Acting Inhibitors against EGFR  and HER2