Molecular docking studies of the following components: cis-abienol, trans-ferruginol, α-cadinol, δ-muurolene and α-pinene were performed to evaluate their binding affinity with the targeted active sites of EGFR, Mcl-1, and caspase-8 proteins. Molecular Operating Environment MOE version 2019.0102 software (Chemical Computing Group, Montreal, Canada) [73 ] was utilized for the docking studies. Protein and ligand structures were prepared as previously described [74 (link)].
The crystal structures of EGFR (PDB: 1M17) [45 (link)], Mcl-1 (PDB: 2NLA) [46 (link)] and caspase-8 (PDB: 1F9E) [47 (link)] were retrieved from the Protein Data Bank (http://www.rcsb.org , accessed on 24 March 2023) [75 ]. The structures of EGFR, MCl-1 and caspase-8 were prepared through the MOE QuickPrep tool.
cis-Abienol, trans-ferruginol, α-cadinol, δ-muurolene, and α-pinene were drawn through the Chemdraw® (PerkinElmer Informatics, Inc., Buckinghamshire, UK), then transferred to the MOE using smiles canonical. The energy of the components was minimized with root mean square (RMS) gradient 0.1 kcal/mol and finally preparing a database file.
The crystal structures of EGFR (PDB: 1M17) [45 (link)], Mcl-1 (PDB: 2NLA) [46 (link)] and caspase-8 (PDB: 1F9E) [47 (link)] were retrieved from the Protein Data Bank (
cis-Abienol, trans-ferruginol, α-cadinol, δ-muurolene, and α-pinene were drawn through the Chemdraw® (PerkinElmer Informatics, Inc., Buckinghamshire, UK), then transferred to the MOE using smiles canonical. The energy of the components was minimized with root mean square (RMS) gradient 0.1 kcal/mol and finally preparing a database file.
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