Detection of Ricin in Plant Extracts and Soil Using Liquid Chromatography–High-Resolution Mass Spectrometry

Браун, А. В.; Taranchenko, V. F.; Tikhomirov, L.A.; Grechukhin, A.P.; Rybal’chenko, I. V.

doi:10.1134/s1061934818080026

Cited by 8 publications

(9 citation statements)

References 12 publications

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“…Recently, one LC-MS method combined with chymotrypsin digestion was developed for identification of ricin [18]. Two specific peptides of C18A (TDVQNRY) and VL-C18B (VL-AATSGNSGTTL) with one missed cleavage site were selected as peptide markers for accurate identification of ricin in plant extracts and soil samples [18]. However, the selected peptide markers are limited for unambiguous identification of ricin in a complicated matrix.…”

Section: Resultsmentioning

confidence: 99%

“…For example, instead of trypsin digestion following the denaturation, reduction and alkylation, the direct trypsin digestion of intact ricin under the solvent-assisted condition was performed with no missed cleavage and reduced digestion time [12,17]. Besides, two peptide markers (C18A and C18B) generated from chymotrypsin digestion were also applied for unambiguous identification of ricin from crude extracts of castor bean and soil samples [18]. However, the selected peptide markers are still relatively limited.…”

Section: Introductionmentioning

confidence: 99%

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LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

Liang¹,

Liu²,

Chen³

et al. 2019

Toxins

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Both ricin and R. communis agglutinin (RCA120), belonging to the type II ribosome-inactivating proteins (RIPs-Ⅱ), are derived from the seeds of the castor bean plant. They share very similar amino acid sequences, but ricin is much more toxic than RCA120. It is urgently necessary to distinguish ricin and RCA120 in response to public safety. Currently, mass spectrometric assays are well established for unambiguous identification of ricin by accurate analysis of differentiated amino acid residues after trypsin digestion. However, diagnostic peptides are relatively limited for unambiguous identification of trace ricin, especially in complex matrices. Here, we demonstrate a digestion strategy of multiple proteinases to produce novel peptide markers for unambiguous identification of ricin. Liquid chromatography-high resolution MS (LC-HRMS) was used to verify the resulting peptides, among which only the peptides with uniqueness and good MS response were selected as peptide markers. Seven novel peptide markers were obtained from tandem digestion of trypsin and endoproteinase Glu-C in PBS buffer. From the chymotrypsin digestion under reduction and non-reduction conditions, eight and seven novel peptides were selected respectively. Using pepsin under pH 1~2 and proteinase K digestion, six and five peptides were selected as novel peptide markers. In conclusion, the obtained novel peptides from the established digestion methods can be recommended for the unambiguous identification of ricin during the investigation of illegal use of the toxin.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

Liang¹,

Liu²,

Chen³

et al. 2019

Toxins

View full text Add to dashboard Cite

show abstract

“…Soil: 2016 discriminating ability of forensic soil analysis techniques including X-ray fluorescence spectrometry (XRF) and element analyzer-isotope ratio mass spectrometry (EA-IRMS) [ 1716 ]; review of soil fingerprinting including uses in forensic and criminal investigations [ 1717 ]; overview of forensic soil examination in Russia [ 1718 ]; 2018 LC/MS method to measure pentobarbital in soils [ 1719 ]; HPLC-HR-MS/MS for detection of ricin in soil [ 1720 ].…”

Section: Miscellaneous Topicsmentioning

confidence: 99%

Interpol review of controlled substances 2016–2019

Jones

Comparin

2020

Forensic Science International: Synergy

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“…Recently, one LC-MS method combined with chymotrypsin digestion was developed for identification of ricin [19]. Two specific peptides of C18A (TDVQNRY) and VL-C18B (VL-AATSGNSGTTL) with one missed cleavage site were selected as peptide markers for accurate identification of ricin in plant extracts and soil samples [19]. However, the selected peptide markers are limited for unambiguous identification of ricin in complicated matrix.…”

Section: Novel Peptide Markers Of Ricin From Chymotrypsin Digestionmentioning

confidence: 99%

“…For example, instead of trypsin digestion following the denaturation, reduction and alkylation, the direct trypsin digestion of intact ricin under the solvent-assisted condition was performed with no missed cleavage and reduced digestion time [13,18]. Besides, two peptide markers (C18A and C18B) generated from chymotrypsin digestion were also applied for unambiguous identification of ricin from crude extracts of castor bean and soil samples [19]. However, the selected peptide markers are still relatively limited.…”

Section: Introductionmentioning

confidence: 99%

LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

Liang¹,

Liu²,

Chen³

et al. 2019

Preprint

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Both ricin and R. communis agglutinin (RCA120), belonging to the type II ribosome-inactivating proteins (RIPs-Ⅱ), are derived from the seeds of castor bean plant. They share very similar amino acid sequences, but ricin is much more toxic than RCA120. It is urgently necessary to distinguish ricin and RCA120 in response to public safety. Currently, mass spectrometric assays are well established for unambiguous identification of ricin by accurate analysis of differentiated amino acid residues after trypsin digestion. However, diagnostic peptides are relatively limited for unambiguous identification of trace ricin, especially in complex matrices. Here, we demonstrate a digestion strategy of multiple proteinases to produce novel peptide markers for unambiguous identification of ricin. LC-HRMS was used to verified the resulting peptides, among which only the peptides with uniqueness and good MS response were selected as peptide markers. Seven novel peptide markers were obtained from tandem digestion of trypsin and endoproteinase Glu-C in PBS buffer. From the chymotrypsin digestion under reduction and non-reduction conditions, eight and seven novel peptides were selected respectively. Using pepsin under pH 1~2 and proteinase K digestion, 6 and 5 peptides were selected as novel peptide markers. In conclusion, the obtained novel peptides from the established digestion methods can be recommended for the unambiguous identification of ricin during the investigation of illegal use of the toxin.

show abstract

Detection of Ricin in Plant Extracts and Soil Using Liquid Chromatography–High-Resolution Mass Spectrometry

Cited by 8 publications

References 12 publications

LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

Interpol review of controlled substances 2016–2019

LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies

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