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

doi:10.5012/bkcs.2014.35.1.250

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 journal › Article › peer-review

3 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	250-252
Number of pages	3
Journal	Bulletin of the Korean Chemical Society
Volume	35
Issue number	1
DOIs	https://doi.org/10.5012/bkcs.2014.35.1.250
Publication status	Published - 2014 Jan 20

All Science Journal Classification (ASJC) codes

Chemistry(all)

Access to Document

10.5012/bkcs.2014.35.1.250

Cite this

@article{1fb0827623f0471cb35d613ce7df2a11,

title = "Darapladib binds to lipoprotein-associated phospholipase A2 with meaningful interactions",

abstract = "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.",

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

year = "2014",

month = jan,

day = "20",

doi = "10.5012/bkcs.2014.35.1.250",

language = "English",

volume = "35",

pages = "250--252",

journal = "Bulletin of the Korean Chemical Society",

issn = "0253-2964",

publisher = "Korean Chemical Society",

number = "1",

}

TY - JOUR

T1 - Darapladib binds to lipoprotein-associated phospholipase A2 with meaningful interactions

AU - Do, Kyoung Rok

AU - Kim, Chul

AU - Chang, Byungha

AU - An, Seong Soo A.

AU - Shin, Jae Min

AU - Yea, Sang Jun

AU - Song, Mi Young

AU - No, Kyoung Tai

AU - Lee, Jee Young

PY - 2014/1/20

Y1 - 2014/1/20

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84892923170&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84892923170&partnerID=8YFLogxK

U2 - 10.5012/bkcs.2014.35.1.250

DO - 10.5012/bkcs.2014.35.1.250

M3 - Article

AN - SCOPUS:84892923170

SN - 0253-2964

VL - 35

SP - 250

EP - 252

JO - Bulletin of the Korean Chemical Society

JF - Bulletin of the Korean Chemical Society

IS - 1

ER -

Darapladib binds to lipoprotein-associated phospholipase A2 with meaningful interactions

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this