Abstract
This work was supported by the National Research Foundation (NRF) of South Africa (Thuthuka grant number 106959), the University of Pretoria (Research and Development Program) and the Council for Scientific and Industrial Research (CSIR), South Africa.
Highlights
Protein-ligand contacts noted during a 100 ns molecular dynamic (MD) simulation at 310 K for two different enantiomers of 19 (S,R and S,S) bound to BACE1 in the confirmed binding pose
The root-mean-square deviation (RMSD) of the ligands during the simulation show pose A to be stable in the binding pocket with an RMSD of 2 Å, while pose B is unstable with significant movement of the ligand in relation to the backbone
Computational studies were performed to identify the correct binding pose of a series of carbazole-based BACE1 inhibitors as there was no clear consensus on the correct pose based on previously reported studies
Summary
Protein-ligand contacts noted during a 100 ns MD simulation at 310 K for two different enantiomers of 19 (S,R and S,S) bound to BACE1 in the confirmed binding pose.
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