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• Jiang, J
• Kang, H
• Song, X
• Huang, S
• Li, S
• Xu, J
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• Jiang, J
• Kang, H
• Song, X
• Huang, S
• Li, S
• Xu, J
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• Jiang, J
• Kang, H
• Song, X
• Huang, S
• Li, S
• Xu, J

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Int. J. Mol. Sci. 2013, 14(1), 807-817; doi:10.3390/ijms14010807

Article

A Model of Interaction between Nicotinamide Adenine Dinucleotide Phosphate (NADPH) Oxidase and Apocynin Analogues by Docking Method

Jie Jiang ¹ , Hongjun Kang ^1,† , Xiaoliang Song ^1,† , Sichao Huang ¹ , Sha Li ^1,*  and Jun Xu ^2,*

¹ College of Pharmacy, Jinan University, Guangzhou 510632, China ² College of Medicine, Jinan University, Guangzhou 510632, China ^† These authors contributed equally to this work.

* Authors to whom correspondence should be addressed.

Received: 14 November 2012; in revised form: 11 December 2012 / Accepted: 24 December 2012 / Published: 4 January 2013

(This article belongs to the Section Molecular Recognition)

Download PDF Full-Text [309 KB, uploaded 4 January 2013 15:36 CET]

Abstract: Some apocynin analogues have exhibited outstanding inhibition to NADPH oxidase. In this study, the key interactions between apocynin analogues and NADPH oxidase were analyzed by the docking method. The potential active site was first identified by the SiteID program combining with the key residue CYS378. Afterwards, the compounds in the training set were docked into NADPH oxidase (1K4U) under specific docking constraints to discuss the key interactions between ligands and the receptor. These key interactions were then validated by the consistence between the docking result and the experimental result of the test set. The result reveals that the Pi interaction between apocynin analogues and NADPH oxidase has a direct contribution to inhibition activities, except for H-bond formation and docking score. The key interactions might be valuable to discover and screen apocynin analogues as potent inhibitors of NADPH oxidase.

Keywords: NADPH oxidase; apocynin analogues; inhibitor; docking

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