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通过竞争性 ABPP 揭示农用化学品对植物丝氨酸水解酶的选择性抑制。

Selective inhibition of plant serine hydrolases by agrochemicals revealed by competitive ABPP.

机构信息

The Plant Chemetics Laboratory, Chemical Genomics Centre of the Max Planck Society, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, D-50829 Cologne, Germany.

出版信息

Bioorg Med Chem. 2012 Jan 15;20(2):597-600. doi: 10.1016/j.bmc.2011.06.040. Epub 2011 Jul 18.

Abstract

Organophosphate and -phosphonates and their thio derivatives are often used in agroindustry as herbicides and insecticides, but their potential off-targets in the plant are poorly investigated. Here, we use competitive activity-based protein profiling (ABPP) of serine hydrolases (SHs) to detect targets of these agrochemicals and other compounds in Arabidopsis thaliana. Using broad-range and specific probes, and by overexpression of various SHs in planta, we are able to confirm eight SH-compound interactions, including selective inhibition of carboxylesterase CXE12, prolyloligopeptidase, methylesterase MES2 and tripeptidyl peptidase TPP2. These observations can be used for the design of novel probes and selective inhibitors and may help to assess physiological effects of agrochemicals on crop plants.

摘要

有机磷和有机膦酸酯及其硫代衍生物通常在农业工业中用作除草剂和杀虫剂,但它们在植物中的潜在非靶标还未被充分研究。在这里,我们使用基于竞争的活性的丝氨酸水解酶(SH)的蛋白质组学(ABPP)来检测这些农业化学品和其他化合物在拟南芥中的靶标。使用广谱和特异性探针,并通过在植物体内过表达各种 SH,我们能够确认八种 SH-化合物相互作用,包括对羧酸酯酶 CXE12、脯氨酰寡肽酶、甲酯酶 MES2 和三肽基肽酶 TPP2 的选择性抑制。这些观察结果可用于设计新型探针和选择性抑制剂,并可能有助于评估农业化学品对作物的生理影响。

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