Cargando…
Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis
The non-protein amino acid β-methylamino-L-alanine (BMAA) has been linked to neurodegenerative disease and reported throughout the environment. Proposed mechanisms of bioaccumulation, trophic transfer and chronic toxicity of BMAA rely on the hypothesis of protein misincorporation. Poorly selective m...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5758758/ https://www.ncbi.nlm.nih.gov/pubmed/29311581 http://dx.doi.org/10.1038/s41598-017-18392-w |
_version_ | 1783291056040706048 |
---|---|
author | Beach, Daniel G. Kerrin, Elliott S. Giddings, Sabrina D. Quilliam, Michael A. McCarron, Pearse |
author_facet | Beach, Daniel G. Kerrin, Elliott S. Giddings, Sabrina D. Quilliam, Michael A. McCarron, Pearse |
author_sort | Beach, Daniel G. |
collection | PubMed |
description | The non-protein amino acid β-methylamino-L-alanine (BMAA) has been linked to neurodegenerative disease and reported throughout the environment. Proposed mechanisms of bioaccumulation, trophic transfer and chronic toxicity of BMAA rely on the hypothesis of protein misincorporation. Poorly selective methods for BMAA analysis have led to controversy. Here, a recently reported highly selective method for BMAA quantitation using hydrophilic interaction liquid chromatography-differential mobility spectrometry-tandem mass spectrometry (HILIC-DMS-MS/MS) is expanded to include proteinogenic amino acids from hydrolyzed biological samples. For BMAA quantitation, we present a double spiking isotope dilution approach using D(3)-BMAA and (13)C(15)N(2)-BMAA. These methods were applied to study release of BMAA during acid hydrolysis under a variety of conditions, revealing that the majority of BMAA can be extracted along with only a small proportion of protein. A time course hydrolysis of BMAA from mussel tissue was carried out to assess the recovery of BMAA during sample preparation. The majority of BMAA measured by typical methods was released before a significant proportion of protein was hydrolyzed. Little change was observed in protein hydrolysis beyond typical hydrolysis times but the concentration of BMAA increased linearly. These findings demonstrate protein misincorporation is not the predominant form of BMAA in cycad and shellfish. |
format | Online Article Text |
id | pubmed-5758758 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-57587582018-01-10 Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis Beach, Daniel G. Kerrin, Elliott S. Giddings, Sabrina D. Quilliam, Michael A. McCarron, Pearse Sci Rep Article The non-protein amino acid β-methylamino-L-alanine (BMAA) has been linked to neurodegenerative disease and reported throughout the environment. Proposed mechanisms of bioaccumulation, trophic transfer and chronic toxicity of BMAA rely on the hypothesis of protein misincorporation. Poorly selective methods for BMAA analysis have led to controversy. Here, a recently reported highly selective method for BMAA quantitation using hydrophilic interaction liquid chromatography-differential mobility spectrometry-tandem mass spectrometry (HILIC-DMS-MS/MS) is expanded to include proteinogenic amino acids from hydrolyzed biological samples. For BMAA quantitation, we present a double spiking isotope dilution approach using D(3)-BMAA and (13)C(15)N(2)-BMAA. These methods were applied to study release of BMAA during acid hydrolysis under a variety of conditions, revealing that the majority of BMAA can be extracted along with only a small proportion of protein. A time course hydrolysis of BMAA from mussel tissue was carried out to assess the recovery of BMAA during sample preparation. The majority of BMAA measured by typical methods was released before a significant proportion of protein was hydrolyzed. Little change was observed in protein hydrolysis beyond typical hydrolysis times but the concentration of BMAA increased linearly. These findings demonstrate protein misincorporation is not the predominant form of BMAA in cycad and shellfish. Nature Publishing Group UK 2018-01-08 /pmc/articles/PMC5758758/ /pubmed/29311581 http://dx.doi.org/10.1038/s41598-017-18392-w Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Beach, Daniel G. Kerrin, Elliott S. Giddings, Sabrina D. Quilliam, Michael A. McCarron, Pearse Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title | Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title_full | Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title_fullStr | Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title_full_unstemmed | Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title_short | Differential Mobility-Mass Spectrometry Double Spike Isotope Dilution Study of Release of β-Methylaminoalanine and Proteinogenic Amino Acids during Biological Sample Hydrolysis |
title_sort | differential mobility-mass spectrometry double spike isotope dilution study of release of β-methylaminoalanine and proteinogenic amino acids during biological sample hydrolysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5758758/ https://www.ncbi.nlm.nih.gov/pubmed/29311581 http://dx.doi.org/10.1038/s41598-017-18392-w |
work_keys_str_mv | AT beachdanielg differentialmobilitymassspectrometrydoublespikeisotopedilutionstudyofreleaseofbmethylaminoalanineandproteinogenicaminoacidsduringbiologicalsamplehydrolysis AT kerrinelliotts differentialmobilitymassspectrometrydoublespikeisotopedilutionstudyofreleaseofbmethylaminoalanineandproteinogenicaminoacidsduringbiologicalsamplehydrolysis AT giddingssabrinad differentialmobilitymassspectrometrydoublespikeisotopedilutionstudyofreleaseofbmethylaminoalanineandproteinogenicaminoacidsduringbiologicalsamplehydrolysis AT quilliammichaela differentialmobilitymassspectrometrydoublespikeisotopedilutionstudyofreleaseofbmethylaminoalanineandproteinogenicaminoacidsduringbiologicalsamplehydrolysis AT mccarronpearse differentialmobilitymassspectrometrydoublespikeisotopedilutionstudyofreleaseofbmethylaminoalanineandproteinogenicaminoacidsduringbiologicalsamplehydrolysis |