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Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry.
Anal Bioanal Chem. 2007 Nov; 389(6):1901-7.AB

Abstract

A liquid chromatography-electrospray-tandem mass spectrometry (LC-ESI-MS-MS) method based on the detection of biomarker peptides from allergenic proteins was devised for confirming and quantifying peanut allergens in foods. Peptides obtained from tryptic digestion of Ara h 2 and Ara h 3/4 proteins were identified and characterized by LC-MS and LC-MS-MS with a quadrupole-time of flight mass analyzer. Four peptides were chosen and investigated as biomarkers taking into account their selectivity, the absence of missed cleavages, the uniform distribution in the Ara h 2 and Ara h 3/4 protein isoforms together with their spectral features under ESI-MS-MS conditions, and good repeatability of LC retention time. Because of the different expression levels, the selection of two different allergenic proteins was proved to be useful in the identification and univocal confirmation of the presence of peanuts in foodstuffs. Using rice crisp and chocolate-based snacks as model food matrix, an LC-MS-MS method with triple quadrupole mass analyzer allowed good detection limits to be obtained for Ara h 2 (5 microg protein g(-1) matrix) and Ara h 3/4 (1 microg protein g(-1) matrix). Linearity of the method was established in the 10-200 microg g(-1) range of peanut proteins in the food matrix investigated. Method selectivity was demonstrated by analyzing tree nuts (almonds, pecan nuts, hazelnuts, walnuts) and food ingredients such as milk, soy beans, chocolate, cornflakes, and rice crisp.

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Authors+Show Affiliations

Careri M
Dipartimento di Chimica Generale ed Inorganica, Chimica Analitica, Chimica Fisica, Università degli Studi di Parma, Viale Usberti 17/A, 43100 Parma, Italy.
Costa A
No affiliation info available
Elviri L
No affiliation info available
Lagos JB
No affiliation info available
Mangia A
No affiliation info available
Terenghi M
No affiliation info available
Cereti A
No affiliation info available
Garoffo LP
No affiliation info available

MeSH

2S Albumins, PlantAllergensAntigens, PlantBiomarkersChromatography, LiquidFood AnalysisGlycoproteinsPeptide FragmentsPlant ProteinsProtein IsoformsSeed Storage ProteinsTandem Mass SpectrometryTime Factors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17899033

Citation

Careri, M, et al. "Use of Specific Peptide Biomarkers for Quantitative Confirmation of Hidden Allergenic Peanut Proteins Ara H 2 and Ara H 3/4 for Food Control By Liquid Chromatography-tandem Mass Spectrometry." Analytical and Bioanalytical Chemistry, vol. 389, no. 6, 2007, pp. 1901-7.
Careri M, Costa A, Elviri L, et al. Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry. Anal Bioanal Chem. 2007;389(6):1901-7.
Careri, M., Costa, A., Elviri, L., Lagos, J. B., Mangia, A., Terenghi, M., Cereti, A., & Garoffo, L. P. (2007). Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry. Analytical and Bioanalytical Chemistry, 389(6), 1901-7.
Careri M, et al. Use of Specific Peptide Biomarkers for Quantitative Confirmation of Hidden Allergenic Peanut Proteins Ara H 2 and Ara H 3/4 for Food Control By Liquid Chromatography-tandem Mass Spectrometry. Anal Bioanal Chem. 2007;389(6):1901-7. PubMed PMID: 17899033.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry. AU - Careri,M, AU - Costa,A, AU - Elviri,L, AU - Lagos,J-B, AU - Mangia,A, AU - Terenghi,M, AU - Cereti,A, AU - Garoffo,L Perono, Y1 - 2007/09/27/ PY - 2007/07/03/received PY - 2007/08/31/accepted PY - 2007/08/30/revised PY - 2007/9/28/pubmed PY - 2008/2/9/medline PY - 2007/9/28/entrez SP - 1901 EP - 7 JF - Analytical and bioanalytical chemistry JO - Anal Bioanal Chem VL - 389 IS - 6 N2 - A liquid chromatography-electrospray-tandem mass spectrometry (LC-ESI-MS-MS) method based on the detection of biomarker peptides from allergenic proteins was devised for confirming and quantifying peanut allergens in foods. Peptides obtained from tryptic digestion of Ara h 2 and Ara h 3/4 proteins were identified and characterized by LC-MS and LC-MS-MS with a quadrupole-time of flight mass analyzer. Four peptides were chosen and investigated as biomarkers taking into account their selectivity, the absence of missed cleavages, the uniform distribution in the Ara h 2 and Ara h 3/4 protein isoforms together with their spectral features under ESI-MS-MS conditions, and good repeatability of LC retention time. Because of the different expression levels, the selection of two different allergenic proteins was proved to be useful in the identification and univocal confirmation of the presence of peanuts in foodstuffs. Using rice crisp and chocolate-based snacks as model food matrix, an LC-MS-MS method with triple quadrupole mass analyzer allowed good detection limits to be obtained for Ara h 2 (5 microg protein g(-1) matrix) and Ara h 3/4 (1 microg protein g(-1) matrix). Linearity of the method was established in the 10-200 microg g(-1) range of peanut proteins in the food matrix investigated. Method selectivity was demonstrated by analyzing tree nuts (almonds, pecan nuts, hazelnuts, walnuts) and food ingredients such as milk, soy beans, chocolate, cornflakes, and rice crisp. SN - 1618-2642 UR - https://www.unboundmedicine.com/medline/citation/17899033/Use_of_specific_peptide_biomarkers_for_quantitative_confirmation_of_hidden_allergenic_peanut_proteins_Ara_h_2_and_Ara_h_3/4_for_food_control_by_liquid_chromatography_tandem_mass_spectrometry_ L2 - https://dx.doi.org/10.1007/s00216-007-1595-2 DB - PRIME DP - Unbound Medicine ER -