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AbstractAbstract
[en] Lipoprotein-associated phospholipase A2 (Lp-PLA2) is a crucial enzyme in atherosclerosis as a potential drug target. The most remarkable Lp-PLA2 inhibitory drug is Darapladib. We determined the binding pose of Darapladib to Lp-PLA2 through docking study. Darapladib formed two hydrogen bonding interactions with the side chain of Tyr160 and Gln352 and several pi-pi interactions with aromatic and aliphatic hydrophobic residues of Lp-PLA2. It is known that the dietylpropan-amine moiety of Darapladib has influence on the improvement of its oral bioavailability and we supposed this in our docking results
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22 refs, 3 figs
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Journal Article
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Bulletin of the Korean Chemical Society; ISSN 0253-2964; ; v. 35(1); p. 250-252
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