کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1369601 | 981784 | 2012 | 8 صفحه PDF | دانلود رایگان |
A series of N-formyl-α-amino acid esters of β-lactone derivatives structurally related to tetrahydrolipstatin (THL) and O-3841 were synthesized that inhibit human and murine diacylglycerol lipase (DAGL) activities. New ether lipid reporter compounds were developed for an in vitro assay to efficiently screen inhibitors of 1,2-diacyl-sn-glycerol hydrolysis and related lipase activities using fluorescence resonance energy transfer (FRET). A standardized thin layer chromatography (TLC) radioassay of diacylglycerol lipase activity utilizing the labeled endogenous substrate [1″-14C]1-stearoyl-2-arachidonoyl-sn-glycerol with phosphorimaging detection was used to quantify inhibition by following formation of the initial product [1″-14C]2-arachidonoylglycerol and further hydrolysis under the assay conditions to [1-14C]arachidonic acid.
New N-formyl-α-amino acid analogs of tetrahydrolipstatin (THL) were synthesized that inhibit human and murine diacylglycerol lipases. New reporter compounds were developed to screen inhibitors of 1,2-diacyl-sn-glycerol hydrolysis activity using fluorescence resonance energy transfer (FRET). Diacylglycerol lipase (DAGL) activities were quantified using [1″-14C]1-stearoyl-2-arachidonoyl-sn-glycerol substrate in a thin layer chromatography (TLC) assay using phosphorimaging analysis.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 22, Issue 14, 15 July 2012, Pages 4585–4592