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. 2025 Aug 22;15:30856. doi: 10.1038/s41598-025-10857-7

Table 7.

Binding pockets and functional outcomes of Phytochemical-Protein Interactions.

Target protein Binding pocket characteristics Eugenol 3-Allyl-6-methoxyphenol Caryophyllene Phenol, 2-methoxy-4-(2-propenyl) 3-Allyl-6-methoxyphenyl acetate Bis(2-ethylhexyl) phthalate
Cytochrome P450 Hydrophobic cleft with heme coordination Blocks catalytic site (potential inhibitor) Moderate inhibition Strong hydrophobic interference Competitive inhibition Weak binding, minimal effect Steric hindrance, substrate exclusion
Ecdysone 20-monooxygenase isoform X1 Steroid-binding hydrophobic pocket Disrupts substrate binding Partial inhibition Strong allosteric modulation Competitive inhibition Weak binding, no effect Competitive inhibition
Muscle calcium channel subunit alpha-1 Voltage-sensing domain (hydrophobic) Weak allosteric modulation Channel blocking Strong allosteric inhibition Stabilizes inactive state Minimal modulation Blocks ion conduction
Odorant binding protein 2 Aromatic/hydrophobic ligand-binding site Competitive binding (odor masking) Weak displacement of native ligands Irreversible binding (odor suppression) Competitive binding No significant effect Strong competitive binding
Gamma-aminobutyric acid receptor subunit beta Extracellular ligand-binding domain Weak antagonism Minimal modulation Allosteric inhibition Weak binding No effect Weak antagonism
Vitellogenin domain-containing protein Lipid-binding pocket Disrupts protein-lipid interactions Weak binding Strong lipid displacement Alters structural stability No significant effect Competes with endogenous lipids
Gustatory receptor Bitter-taste receptor pocket (hydrophobic) Taste modulation Partial agonist Strong antagonism (taste suppression) Competitive binding Weak interaction Irreversible binding