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Fig 1.

Two-dimensional chemical structures of Allium sativum L.-derived compounds investigated for their inhibitory potential and physicochemical properties.

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Fig 2.

Co-crystallized ligands of the selected macromolecular targets.

The ligand-receptor pairs include CDK2/DTQ, CDK6/FSE, Topoisomerase I/EDH, Topoisomerase II/ANP, G-Quadruplex/PYN, Bcl-2/LIO, and XIAP-Bir2/1RH. These ligands are established inhibitors of their respective targets and were used to validate docking protocols.

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Fig 3.

Conformational clustering of co-crystal ligands used to validate molecular docking parameters.

The RMSD was calculated between the original co-crystal ligand positions (green-colored aromatic carbons) and their docked poses (cyan-colored aromatic carbons). A cut-off RMSD value of 2.0 Å was applied to identify closely related conformers, indicating acceptable docking accuracy.

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Table 1.

Binding energy (ΔG, kcal/mol) and inhibition constant (Ki, μM) of organosulfur compounds from Allium sativum L. docked against selected macromolecular targets.

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Fig 4.

Binding modes and LigPlot+ molecular interactions of the best-docked investigational ligands with their molecular targets.

Bond lengths shown in Å and hydrogen bonding angles between the ligands and key amino acid or nucleotide residues of the receptors are annotated on the LigPlot+ and binding mode images respectively. Z-ajoene (cpd1) showed notable binding with Bcl-2 (Panel 4a), CDK2 (Panel 4b), and Topoisomerase II (Panel 4f) through a combination of hydrogen bonding and hydrophobic interactions. S-allyl-L-cysteine (cpd6) demonstrated strong interactions with G-Quadruplex (Panel 4d), Topoisomerase I (Fig 4e), VEGFR2 (Panel 4g), XIAP-Bir2 (Panel 4h), and CDK-6 (Panel 4c), involving hydrogen bonds and multiple hydrophobic contacts. Specific interacting residues and bond types are highlighted in each panel (Panel 4a-4h).

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Fig 5.

Post-docking energy minimization using OpenBabel tool.

Energy values showed that ligand-receptor complexes have lower energy post-docking minimization (Panel 5a). An RMSD value of 2.0 Å was considered as cut-off for ligands that remain in similar poses after aligning pre-energy minimization complexes (green colored carbon backbone) with post-docking energy minimization complexes (cyan colored carbon backbone) (Panel 5b-j). Complexes: Cpd1/Bcl2 (Panel 5c), Cpd1/Cdk2 (Panel 5d), Cpd6/Cdk6 (Panel 5e), Cpd6/G-Quadruplex (Panel 5f), Cpd6/Topoisomerase II (Panel 5g), Cpd1/Topoisomerase I (Fig 5h), Cpd6/VEGFR2 (Panel 5i) and Cpd6/XIAP Bir2 (Panel 5j).

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Table 2.

Predicted physicochemical properties of the investigational bioactive compounds calculated using the Molinspiration web server.

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Table 3.

Physicochemical properties of the investigational compounds calculated using DataWarrior software.

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Table 4.

Oral bioavailability of the selected compounds based on Veber and Egan Rules as predicted by the SwissADME server.

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Table 5.

Absorption, distribution, elimination, and toxicity profiles of the bioactive compounds assessed using PreADME; CYP2C19 and CYP2C9 inhibition predicted by SwissADME.

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