Identification of organophosphate modifications by high-resolution mass spectrometry

Jun Hyung Lee; Wooyoung Eric Jang; Ji Hwan Park; Hazara Begum Mohammad; Jin Young Lee; Woo Hyeon Jeong; Min Sik Kim

doi:10.1002/bkcs.12478

Identification of organophosphate modifications by high-resolution mass spectrometry

Jun Hyung Lee, Wooyoung Eric Jang, Ji Hwan Park, Hazara Begum Mohammad, Jin Young Lee, Woo Hyeon Jeong, Min Sik Kim

Department of New Biology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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.

Original language	English
Pages (from-to)	444-449
Number of pages	6
Journal	Bulletin of the Korean Chemical Society
Volume	43
Issue number	3
DOIs	https://doi.org/10.1002/bkcs.12478
State	Published - Mar 2022

Bibliographical note

Publisher Copyright:
© 2022 Korean Chemical Society, Seoul & Wiley-VCH GmbH

Keywords

human plasma
mass spectrometry
nuerotoxicity
organophosphate
protein modification

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10.1002/bkcs.12478

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title = "Identification of organophosphate modifications by high-resolution mass spectrometry",

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.",

keywords = "human plasma, mass spectrometry, nuerotoxicity, organophosphate, protein modification",

author = "Lee, {Jun Hyung} and Jang, {Wooyoung Eric} and Park, {Ji Hwan} and Mohammad, {Hazara Begum} and Lee, {Jin Young} and Jeong, {Woo Hyeon} and Kim, {Min Sik}",

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year = "2022",

month = mar,

doi = "10.1002/bkcs.12478",

language = "English",

volume = "43",

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TY - JOUR

T1 - Identification of organophosphate modifications by high-resolution mass spectrometry

AU - Lee, Jun Hyung

AU - Jang, Wooyoung Eric

AU - Park, Ji Hwan

AU - Mohammad, Hazara Begum

AU - Lee, Jin Young

AU - Jeong, Woo Hyeon

AU - Kim, Min Sik

PY - 2022/3

Y1 - 2022/3

N2 - 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.

AB - 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.

KW - human plasma

KW - mass spectrometry

KW - nuerotoxicity

KW - organophosphate

KW - protein modification

UR - http://www.scopus.com/inward/record.url?scp=85122970787&partnerID=8YFLogxK

U2 - 10.1002/bkcs.12478

DO - 10.1002/bkcs.12478

M3 - Article

AN - SCOPUS:85122970787

SN - 0253-2964

VL - 43

SP - 444

EP - 449

JO - Bulletin of the Korean Chemical Society

JF - Bulletin of the Korean Chemical Society

IS - 3

ER -

Identification of organophosphate modifications by high-resolution mass spectrometry

Abstract

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Keywords

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