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The spurge hawkmoth Hyles euphorbiae (Lepidoptera, Sphingidae) is an insect herbivore feeding exclusively on spurges (Euphorbia). These are toxic due to their secondary metabolites including diterpene esters with numerous harmful biological activities, preventing their use by most herbivores. Extracts of frass from H. euphorbiae and of its main larval food plant in Central Europe, the cypress spurge (Euphorbia cyparissias L.), were analyzed via liquid chromatography using a triple-quadrupole (MS/MS) and a high-resolution–quadrupole time-of-flight mass spectrometer (QTOF-MS). We report for the first time the finding of the tigliane (phorbol ester) phorbol-13-acetate and two 12-O-tetradecanoylphorbol-13-acetate (TPA) isomers of unknown structure (compounds 2 and 3) in E. cyparissias. Our data support the assignment of these two compounds as tiglianes and are therefore referred to by us as “putative tiglianes”. Additionally, the distribution of the three reported compounds within the plant parts (leaves, stem and root) was analyzed to gain first insights into the metabolite conditions H. euphorbiae copes with in nature. Phorbol-13-acetate was detected in the plant’s root only, while the other compounds were observed in all three plant parts, although in different distributions. Moreover, our results indicate that the occurrence of compound 3 rises upon larval feeding. Finally, the presence of the plant-derived putative tiglianes in frass from E. cyparissias leaves feeding larvae is confirmed, corroborating the close plant–herbivore interaction.

Bromodomain and extra-terminal domain (BET) family proteins have become a hot research area because of their close relationship with a variety of human diseases. The non-invasive imaging technique, such as positron emission tomography (PET), provides a powerful tool to visualize and quantify the BET family proteins that accelerating the investigation of this domain. Herein, we describe the development of a promising PET probe, [11C]1, specifically targeting BET family proteins based on the potent BET inhibitor CF53. [11C]1 was successfully radio-synthesized with good yield and high purity after the optimization of radiolabeling conditions. The in vivo bio-activities evaluation of [11C]1 was performed using PET imaging in rodents. The results demonstrated that [11C]1 has favorable uptake in peripheral organs and moderate uptake in the brain. Further blocking studies indicated the high binding specificity and selectivity for BET proteins of this probe. Our findings suggest that [11C]1 is a promising BET PET probe for BET proteins as well as epigenetic imaging.