Docking score of secondary metabolites of <i>Trichoderma</i> spp. against EGFR tyrosine kinase domain.

Docking score of secondary metabolites of Trichoderma spp. against EGFR tyrosine kinase domain.</p

Physicochemical properties of lead metabolites of <i>Trichoderma</i> spp. and standard inhibitor.

Physicochemical properties of lead metabolites of Trichoderma spp. and standard inhibitor.</p

Predicted pharmacokinetic and toxicity properties of lead metabolites of <i>Trichoderma</i> spp. and standard inhibitor.

Predicted pharmacokinetic and toxicity properties of lead metabolites of Trichoderma spp. and standard inhibitor.</p

Visualization of MD simulation trajectory plots of EGFR tyrosine kinase domain in unbound, lead metabolite (Aspochalasin M) bound and standard inhibitor (Erlotinib) bound complex during 100 ns MD simulation period.

A: RMSD; B: RMSF; C: SASA; D: Rg and E: Hydrogen bond formation. Green: unbound EGFR tyrosine kinase domain, orange: EGFR tyrosine kinase domain-Aspochalasin M complex and purple: EGFR tyrosine kinase domain-Erlotinib complex.</p

Structural similarity of 200 compounds and standard drug used in the study.

Lines between the dots represent the structurally similar compounds and the numbers on each dot represent the compound name, as listed in S1 Table.</p

Structure of lead metabolites of <i>Trichoderma</i> spp. and standard inhibitor having the potential to bind at the active binding sites of EGFR tyrosine kinase domain.

Structure of lead metabolites of Trichoderma spp. and standard inhibitor having the potential to bind at the active binding sites of EGFR tyrosine kinase domain.</p

Binding free energy calculations of EGFR tyrosine kinase complexed with the lead metabolite of <i>Trichoderma</i> spp. and standard inhibitor.

Binding free energy calculations of EGFR tyrosine kinase complexed with the lead metabolite of Trichoderma spp. and standard inhibitor.</p

2D interaction of lead metabolites of <i>Trichoderma</i> spp. and standard inhibitor at the active binding sites of EGFR tyrosine kinase domain.

2D interaction of lead metabolites of Trichoderma spp. and standard inhibitor at the active binding sites of EGFR tyrosine kinase domain.</p

Fig 5 -

BOILED-Egg diagram (A) and bioavailability radar map (B) of lead metabolites of Trichoderma spp. and standard inhibitor. The pink region within the hexagon shows the optimal range of each drug-likeness property. Lipophilicity (LIPO) as XLOGP3 is ranged between −0.7 and +5.0, molecular weight (SIZE) is ranged between 150 and 500 g/mol and polar surface area (POLAR) as topological polar surface area (TPSA) is ranged between 20 and 130 Å2), insolubility (INSOLU) in water by log S scale is not > 6, in saturation (INSATU) as the fraction of carbons in sp3 hybridization is ranged between 0.25 and 1, and flexibility (FLEX) of rotatable bonds is not > 9 [23].</p

3D interaction of lead metabolites of <i>Trichoderma</i> spp. and standard inhibitor at the active binding sites of EGFR tyrosine kinase domain.

3D interaction of lead metabolites of Trichoderma spp. and standard inhibitor at the active binding sites of EGFR tyrosine kinase domain.</p