Abstract
In the present work, a molecular docking approach was conducted to investigate the antimalarial activity of neolignan derivatives with 4-methoxybenzoyl substituent (N1-N10) against chloroquine-sensitive and -resistant proteins. It was found that the neolignan derivatives were able to interact with the amino acid residues of Ala16, and Ser167/Tyr170 in the active site of the chloroquine-sensitive protein. On the other hand, the interactions of the neolignan derivatives with Arg59, Arg122, and Phe116/Ser120 residues were observed in the active site of the chloroquine-resistant protein. Most neolignan derivatives had stronger interaction than the native ligands in the active sites of both proteins. Among the evaluated neolignan derivatives, N9 and N8 compounds gave the strongest binding energy against the active sites of chloroquine-sensitive and -resistant proteins, respectively. These findings demonstrate that the presence of the nitro group in the neolignan structure is crucial for its inhibitory activity against chloroquine-sensitive and -resistant proteins.
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