Abstract
Darapladib is one of the most potent Lp-PLA2 (Lipoprotein-associated phospholipase A2) inhibitor with an IC50 of 0.25 nM. We demonstrate that a crucial step of Darapladib synthesis was not correctly described in the literature, leading to the production of wrong regioisomers. Moreover we show that the inhibitory activity is directly linked to the position on N1 since compounds bearing alkylation on different sites have potentially less interaction within the active site of Lp-PLA2.
Keywords:
Atherosclerosis; Darapladib; Lp-PLA(2); Regioselectivity; Thiouracil.
Copyright © 2017 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Alkyl-2-acetylglycerophosphocholine Esterase / antagonists & inhibitors
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1-Alkyl-2-acetylglycerophosphocholine Esterase / chemistry
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Alkylation
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Benzaldehydes / chemical synthesis
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Benzaldehydes / chemistry*
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Benzaldehydes / pharmacology
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Catalytic Domain
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Humans
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Isomerism
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Oximes / chemical synthesis
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Oximes / chemistry*
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Oximes / pharmacology
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Phospholipase A2 Inhibitors / chemical synthesis
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Phospholipase A2 Inhibitors / chemistry*
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Phospholipase A2 Inhibitors / pharmacology
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Thiouracil / chemistry*
Substances
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Benzaldehydes
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Oximes
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Phospholipase A2 Inhibitors
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Thiouracil
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1-Alkyl-2-acetylglycerophosphocholine Esterase
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darapladib