Alkylated albumin-derived dipeptide C(-HETE)P derivatized by propionic anhydride as a biomarker for the verification of poisoning with sulfur mustard.
Biomarker
Chemical warfare agent
HETE moiety
Propionic anhydride
Protein adduct
Verification
Journal
Analytical and bioanalytical chemistry
ISSN: 1618-2650
Titre abrégé: Anal Bioanal Chem
Pays: Germany
ID NLM: 101134327
Informations de publication
Date de publication:
Aug 2021
Aug 2021
Historique:
received:
29
04
2021
accepted:
04
06
2021
revised:
25
05
2021
pubmed:
4
7
2021
medline:
21
10
2021
entrez:
3
7
2021
Statut:
ppublish
Résumé
Sulfur mustard (SM) is a banned chemical warfare agent recently used in the Syrian Arab Republic conflict causing erythema and blisters characterized by complicated and delayed wound healing. For medical and legal reasons, the proof of exposure to SM is of high toxicological and forensic relevance. SM reacts with endogenous human serum albumin (HSA adducts) alkylating the thiol group of the cysteine residue C
Identifiants
pubmed: 34215915
doi: 10.1007/s00216-021-03454-w
pii: 10.1007/s00216-021-03454-w
pmc: PMC8318952
doi:
Substances chimiques
Albumins
0
Anhydrides
0
Biomarkers
0
Chemical Warfare Agents
0
Dipeptides
0
Propionates
0
propionic anhydride
E3A2VV18E6
Mustard Gas
T8KEC9FH9P
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4907-4916Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : Research Training Group GRK 2338
Informations de copyright
© 2021. The Author(s).
Références
Kehe K, Szinicz L. Medical aspects of sulphur mustard poisoning. Toxicology. 2005;214:198–209.
doi: 10.1016/j.tox.2005.06.014
Evison D, Hinsley D, Rice P. Chemical weapons. BMJ. 2002;324:332.
doi: 10.1136/bmj.324.7333.332
Quillen C. The Islamic State’s evolving chemical arsenal. Studies in Conflict & Terrorism. 2016;39:1019–30. https://doi.org/10.1080/1057610X.2016.1154364 .
doi: 10.1080/1057610X.2016.1154364
John H, Koller M, Worek F, Thiermann H, Siegert M. Forensic evidence of sulfur mustard exposure in real cases of human poisoning by detection of diverse albumin-derived protein adducts. Arch Toxicol. 2019;93:1881–91.
doi: 10.1007/s00204-019-02461-2
Sezigen S, Ivelik K, Ortatatli M, Almacioglu M, Demirkasimoglu M, Eyison RK, et al. Victims of chemical terrorism, a family of four who were exposed to sulfur mustard. Toxicol Lett. 2019;303:9–15.
doi: 10.1016/j.toxlet.2018.12.006
Bullman T, Kang H. A fifty year mortality follow-up study of veterans exposed to low level chemical warfare agent, mustard gas. Ann Epidemiol. 2000;10:333–8.
doi: 10.1016/S1047-2797(00)00060-0
Blum M-M, Mamidanna RVSM. Analytical chemistry and the Chemical Weapons Convention. Anal Bioanal Chem. 2014;406:5067–9. https://doi.org/10.1007/s00216-014-7931-4 .
doi: 10.1007/s00216-014-7931-4
pubmed: 24928112
John H, van der Schans MJ, Koller M, Spruit HET, Worek F, Thiermann H, et al. Fatal sarin poisoning in Syria 2013: forensic verification within an international laboratory network. Forensic Toxicol. 2018;36:61–71.
doi: 10.1007/s11419-017-0376-7
Steinritz D, Striepling E, Rudolf K-D, Schröder-Kraft C, Püschel K, Hullard-Pulstinger A, et al. Medical documentation, bioanalytical evidence of an accidental human exposure to sulfur mustard and general therapy recommendations. Toxicol Lett. 2016;244:112–20.
doi: 10.1016/j.toxlet.2015.08.1105
Xu H, Nie Z, Zhang Y, Li C, Yue L, Yang W, et al. Four sulfur mustard exposure cases: overall analysis of four types of biomarkers in clinical samples provides positive implication for early diagnosis and treatment monitoring. Toxicol Rep. 2014;1:533–43.
doi: 10.1016/j.toxrep.2014.07.017
Noort D, Hulst AG, Trap HC, de Jong LP, Benschop HP. Synthesis and mass spectrometric identification of the major amino acid adducts formed between Sulphur mustard and haemoglobin in human blood. Arch Toxicol. 1997;71:171–8.
doi: 10.1007/s002040050372
Noort D, Fidder A, Hulst AG, de Jong LPA, Benschop HP. Diagnosis and dosimetry of exposure to sulfur mustard: development of a standard operating procedure for mass spectrometric analysis of haemoglobin adducts: exploratory research on albumin and keratin adducts. J Appl Toxicol. 2000;20:S187–S92.
doi: 10.1002/1099-1263(200012)20:1+<::AID-JAT676>3.0.CO;2-F
Zubel T, Hochgesand S, John H, Steinritz D, Schmidt A, Bürkle A, et al. A mass spectrometric platform for the quantitation of sulfur mustard-induced nucleic acid adducts as mechanistically relevant biomarkers of exposure. Arch Toxicol. 2019;93:61–79.
doi: 10.1007/s00204-018-2324-7
Noort D, Hulst AG, de Jong LPA, Benschop HP. Alkylation of human serum albumin by sulfur mustard in vitro and in vivo: mass spectrometric analysis of a cysteine adduct as a sensitive biomarker of exposure. Chem Res Toxicol. 1999;12:715–21.
doi: 10.1021/tx9900369
Benschop HP, van der Schans GP, Noort D, Fidder A, Mars-Groenendijk RH, de Jong LPA. Verification of exposure to sulfur mustard in two casualties of the Iran-Iraq conflict. J Anal Toxicol. 1997;21:249–51. https://doi.org/10.1093/jat/21.4.249 .
doi: 10.1093/jat/21.4.249
pubmed: 9248939
John H, Siegert M, Gandor F, Gawlik M, Kranawetvogl A, Karaghiosoff K, et al. Optimized verification method for detection of an albumin-sulfur mustard adduct at Cys34 using a hybrid quadrupole time-of-flight tandem mass spectrometer after direct plasma proteolysis. Toxicol Lett. 2016;244:103–11.
doi: 10.1016/j.toxlet.2015.09.027
Gandor F, Gawlik M, Thiermann H, John H. Evidence of sulfur mustard exposure in human plasma by LC–ESI–MS–MS detection of the albumin-derived alkylated HETE–CP dipeptide and chromatographic investigation of its cis/trans isomerism. J Anal Toxicol. 2015;39:270–9.
doi: 10.1093/jat/bkv010
John H, Willoh S, Hörmann P, Siegert M, Vondran A, Thiermann H. Procedures for analysis of dried plasma using microsampling devices to detect sulfur mustard albumin adducts for verification of poisoning. Anal Chem. 2016;88:8787–94.
doi: 10.1021/acs.analchem.6b02199
Chen B, Yu H, Liu S, Liu C, Liang L, Li X, et al. A sensitive quantification approach for detection of HETE-CP adduct after benzyl chloroformate derivatization using ultra-high-pressure liquid chromatography tandem mass spectrometry. Anal Bioanal Chem. 2019;411:3405–15.
doi: 10.1007/s00216-019-01820-3
Blum MM, Richter A, Siegert M, Thiermann H, John H. Adduct of the blistering warfare agent sesquimustard with human serum albumin and its mass spectrometric identification for biomedical verification of exposure. Anal Bioanal Chem. 2020;412:7723–37.
doi: 10.1007/s00216-020-02917-w
Blau K, Halket JM, editors. Handbook of derivatives for chromatography. 2nd ed. Chichester: John Wiley & Sons; 1993.
Sethuraman M, McComb ME, Huang H, Huang S, Heibeck T, Costello CE, et al. Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J Proteome Res. 2004;3:1228–33.
doi: 10.1021/pr049887e
Choe L, D'Ascenzo M, Relkin NR, Pappin D, Ross P, Williamson B, et al. 8-Plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease. Proteomics. 2007;7:3651–60.
doi: 10.1002/pmic.200700316
Ross PL, Huang YN, Marchese JN, Williamson B, Parker K, Hattan S, et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics. 2004;3:1154–69. https://doi.org/10.1074/mcp.M400129-MCP200 .
doi: 10.1074/mcp.M400129-MCP200
pubmed: 15385600
Schwarz G, Beck S, Weller MG, Linscheid MW. MeCAT-new iodoacetamide reagents for metal labeling of proteins and peptides. Anal Bioanal Chem. 2011;401:1203.
doi: 10.1007/s00216-011-5189-7
Schmidt A, Kellermann J, Lottspeich F. A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics. 2005;5:4–15.
doi: 10.1002/pmic.200400873
van Faassen M, Bouma G, de Hosson LD, Peters MAM, Kats-Ugurlu G, de Vries EGE, et al. Quantitative profiling of platelet-rich plasma indole markers by direct-matrix derivatization combined with LC-MS/MS in patients with neuroendocrine tumors. Clin Chem. 2019;65:1388–96.
doi: 10.1373/clinchem.2019.305359
Nordström A, Tarkowski P, Tarkowska D, Dolezal K, Åstot C, Sandberg G, et al. Derivatization for LC-electrospray ionization-MS: a tool for improving reversed-phase separation and ESI responses of bases, ribosides, and intact nucleotides. Anal Chem. 2004;76:2869–77.
doi: 10.1021/ac0499017
Pierce WM Jr, Nerland DE. Qualitative and quantitative analyses of phenol, phenylglucuronide, and phenylsulfate in urine and plasma by gas chromatography/mass spectrometry. J Anal Toxicol. 1988;12:344–7.
doi: 10.1093/jat/12.6.344
Escrig-Doménech A, Simó-Alfonso EF, Herrero-Martínez JM, Ramis-Ramos G. Derivatization of hydroxyl functional groups for liquid chromatography and capillary electroseparation. J Chromatogr A. 2013;1296:140–56.
doi: 10.1016/j.chroma.2013.04.027
Brindaba CR, Dey SS, Hajra A. Highly efficient acylation of alcohols, amines and thiols undersolvent-free and catalyst-free conditions. Green Chem. 2003;5:44–6.
doi: 10.1039/b211238h
Work instruction for the reporting of the results of the OPCW biomedical proficiency tests. OPCW; 2020, https://www.opcw.org/sites/default/files/documents/S_series/2017/en/s-1515-2017_e_.pdf , Accessed 02.12.2020.