Identification of organophosphate modifications by high-resolution mass spectrometry
- Title
- Identification of organophosphate modifications by high-resolution mass spectrometry
- Author(s)
- Lee, Jun Hyung ; Jang, Wooyoung Eric ; Park, Jihwan ; Mohammad, Hazara Begum ; Lee, Jin-Young ; Jeong, Woo-Hyeon ; Kim, Min-Sik
- Issued Date
- 2022-03
- Citation
- Bulletin of the Korean Chemical Society, v.43, no.3, pp.444 - 449
- Type
- Article
- Author Keywords
- nuerotoxicity ; organophosphate ; protein modification ; human plasma ; mass spectrometry
- Keywords
- HUMAN SERUM-ALBUMIN ; NERVE AGENTS ; EXPOSURE ; ADDUCTS ; PESTICIDES ; BIOMARKER
- ISSN
- 0253-2964
- Abstract
- Organophosphate (OP) compounds exhibit neurotoxicity by binding to serine residues of acetylcholinesterase (AChE) in the cholinergic nervous system and subsequently lead to the accumulation of acetylcholine in neuromuscular junctions of synapses. AChE capable of hydrolyzing choline esters is known to be inhibited in patients with nerve agents poisoning. Since OP is known to be transported by covalent bonding to human serum albumin (HSA), OP-HSA adducts are considered potential diagnostic markers for OP exposures. In this study, HSA modification sites by OP or OP-like compounds such as V-type (VX) and Novichok-type (A234), insecticide (DFP), and serine protease inhibitor (PMSF) were studied using liquid chromatography-high-resolution tandem mass spectrometry. As a result, we have discovered a novel OP-HSA modification site, Y341. © 2022 Korean Chemical Society, Seoul & Wiley-VCH GmbH
- Publisher
- John Wiley and Sons Inc
- Related Researcher
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Kim, Min-Sik
- Research Interests Cancer Proteogenomics; Biomarker Discovery; Integrative Multi-Omics
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- Appears in Collections:
- Department of New Biology Laboratory for QBIO and Precision Medicine 1. Journal Articles
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