RETRACTED ARTICLE: Suppression of NF-κB signaling by ECN in an arthritic model of inflammation

Table 3 The interaction of the ECN with various protein targets using molecular docking analysis

Ligand-protein interaction	Binding energy (Kcal/mol)	Hydrogen bonds	Hydrogen bond amino acids	Hydrophobic interactions
ECN-JNK	−6.0	1	Arg25	Leu363, Leu23, Lys24, Asn9, Ala510
ECN-NF-κB	−6.0	3	His58, Ser112, Thr60	Ile110
ECN-COX-2	−7.4	2	His2212, Asn2382	Phe2210, His2207, Val2442, Ala2450, His2388, His2386, Ala2446
ECN-TNF-α	−8.1	1	Tyr151	Leu57, Tyr59, Tyr119

The molecular docking analysis showed multiple H-bonds and hydrophobic bonds of the ECN with various protein targets such as JNK, NF-κB, COX-2, and TNF-α. Additionally, the molecular docking analysis also showed the binding energies of the ECN with various protein targets and the amino acid involved in the interaction

ISSN: 2662-7671