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...

Descripción completa

Detalles Bibliográficos
Autores principales: Beach, Daniel G., Kerrin, Elliott S., Giddings, Sabrina D., Quilliam, Michael A., McCarron, Pearse
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