Academic Journals Database
Disseminating quality controlled scientific knowledge

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

ADD TO MY LIST
 
Author(s): Jie Jiang | Hongjun Kang | Xiaoliang Song | Sichao Huang | Sha Li | Jun Xu

Journal: International Journal of Molecular Sciences
ISSN 1422-0067

Volume: 14;
Issue: 1;
Start page: 807;
Date: 2013;
Original page

Keywords: NADPH oxidase | apocynin analogues | inhibitor | docking

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.
Affiliate Program     

Tango Rapperswil
Tango Rapperswil