Darapladib binds to lipoprotein-associated phospholipase A2 with meaningful interactions

Kyoung Rok Do, Chul Kim, Byungha Chang, Seong Soo A. An, Jae Min Shin, Sang Jun Yea, Mi Young Song, Kyoung Tai No, Jee Young Lee

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)250-252
Number of pages3
JournalBulletin of the Korean Chemical Society
Issue number1
Publication statusPublished - 2014 Jan 20

All Science Journal Classification (ASJC) codes

  • Chemistry(all)


Dive into the research topics of 'Darapladib binds to lipoprotein-associated phospholipase A2 with meaningful interactions'. Together they form a unique fingerprint.

Cite this