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While thiol-reactive compounds have been extensively utilized by plants as defensive metabolites, prior investigations into these natural products remained limited. We employed a reactivity-directed analysis method utilizing high-resolution mass spectrometry to conduct thiol reactome profiling on extracts from 70 different plant-derived foods, resulting in the tentative prediction of chemical formulas of 71 abundant molecular adduct ions. Then, we selected a prominent adduct ion for structural elucidation, leading to the identification of ()-dihydromaleimide (DHM) and ()-dihydromaleimide β-d-glucoside (DHMG) in snow pea (). DHM demonstrated insecticidal properties against the fall armyworm (FAW) and and antifeedant activity against FAW, with oxidative stress as a contributing mechanism. Quantitative analyses indicated considerable concentrations of DHMG and DHM in many parts of pea plants and easy conversion of DHMG to DHM in aqueous extracts. This research provided a feasible strategy for the high-throughput screening and discovery of novel botanical natural products for pest control.
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http://dx.doi.org/10.1021/acs.jafc.5c05627 | DOI Listing |
J Agric Food Chem
August 2025
School of Agriculture and Biotechnology, Shenzhen Campus of Sun Yat-sen University, Shenzhen 518107, China.
While thiol-reactive compounds have been extensively utilized by plants as defensive metabolites, prior investigations into these natural products remained limited. We employed a reactivity-directed analysis method utilizing high-resolution mass spectrometry to conduct thiol reactome profiling on extracts from 70 different plant-derived foods, resulting in the tentative prediction of chemical formulas of 71 abundant molecular adduct ions. Then, we selected a prominent adduct ion for structural elucidation, leading to the identification of ()-dihydromaleimide (DHM) and ()-dihydromaleimide β-d-glucoside (DHMG) in snow pea ().
View Article and Find Full Text PDFEnviron Sci Technol
November 2023
Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, Canada.
The precise identification of predominant toxic disinfection byproducts (DBPs) from disinfected water is a longstanding challenge. We propose a new acellular analytical strategy, the 'Thiol Reactome', to identify thiol-reactive DBPs by employing a thiol probe and nontargeted mass spectrometry (MS) analysis. Disinfected/oxidized water samples had reduced cellular oxidative stress responses of 46 ± 23% in Nrf2 reporter cells when preincubated with glutathione (GSH).
View Article and Find Full Text PDFTrends Biochem Sci
May 2022
Department of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg August University Göttingen, Julia-Lermontowa-Weg 3, D-37077 Göttingen, Germany; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. Ele
Modifications of cysteine residues in redox-sensitive proteins are key to redox signaling and stress response in all organisms. A novel type of redox switch was recently discovered that comprises lysine and cysteine residues covalently linked by an nitrogen-oxygen-sulfur (NOS) bridge. Here, we discuss chemical and biological implications of this discovery.
View Article and Find Full Text PDFNeuroscience
January 2014
Department of Clinical Chemistry, University Medical Center Goettingen, Robert-Koch-Str. 40, 37075 Goettingen, Germany. Electronic address:
Numerous studies have provided evidence regarding the involvement of protein S-nitrosylation in the progression of Alzheimer's disease (AD) pathology and its implication in the formation and accumulation of misfolded protein aggregates. The identification of S-nitrosylated proteins can be a major step toward the understanding of mechanisms leading to neuronal degeneration. The present study targeted S-nitrosylated proteins in AD hippocampus, substantia nigra and cortex using the following work-flow that combines S-nitrosothiol-specific antibody detection, classical biotin switch method labeled with fluorescence dye followed by electrospray ionization quadrupole time of flight tandem MS (ESI-QTOF MS/MS) identification.
View Article and Find Full Text PDFClin Proteomics
June 2013
Neurochemistry Research Unit Laboratory, Department of Biochemistry, University of Karachi, Karachi, Pakistan.
Background: Complex molecular events lead to development and progression of liver cirrhosis to HCC. Differentially expressed nuclear membrane associated proteins are responsible for the functional and structural alteration during the progression from cirrhosis to carcinoma. Although alterations/ post translational modifications in protein expression have been extensively quantified, complementary analysis of nuclear membrane proteome changes have been limited.
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