Published January 2014
| Version v1
Journal article
Darapladib Binds to Lipoprotein-Associated Phospholipase A2 with Meaningful Interactions
Creators
- 1. Bioinformatics and Molecular Design Research Center, Seoul (Korea, Republic of)
- 2. Korea Institute of Oriental Medicine, Daejeon (Korea, Republic of)
Description
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
Additional details
Publishing Information
- Journal Title
- Bulletin of the Korean Chemical Society
- Journal Volume
- 35
- Journal Issue
- 1
- Series
- 22 refs, 3 figs
- Journal Page Range
- p. 250-252
- ISSN
- 0253-2964
INIS
- Country of Publication
- Korea, Republic of
- Country of Input or Organization
- Korea, Republic of
- INIS RN
- 46042765
- Subject category
- S37: INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY;
- Descriptors DEI
- AMINES; CHAINS; DRUGS; ENZYMES; HYDROGEN; LIPOPROTEINS; RESIDUES
- Descriptors DEC
- ELEMENTS; LIPIDS; NONMETALS; ORGANIC COMPOUNDS; PROTEINS