Table 4.

Molecular docking of sanguinarine to IκB and NF-κB proteins.

Proteins	Lowest binding energy kcal/mol	Pki (μM)	H-bond	Hydrophobic interaction
IκB	−8.17 ± <0.001	1.03 ± <0.001	Ile94	Leu104, Phe103, Asn105, Gly132, Leu131, Val93, Arg95
NF-κB	−7.27 ± 0.02	4.67 ± 0.19	Ile118	Gly117, Arg35, Ser42, Gly44, Ala43, Arg41

Shown are lowest binding energy, predicted inhibition constant (Pki), amino acids (AA) involved in hydrogen bonding, and hydrophobic interaction. Each docking experiment has been repeated three times.