Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards

Inductively coupled plasma-mass spectrometry (ICP?MS) has been widely used in Life Sciences for the absolute quantification of biomolecules without specific standards, assuming the same response for generic compounds including complex biomolecules. However, contradictory results have been published...

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Detalles Bibliográficos
Autores: Cid-Barrio, Laura, Calderón Celis, Francisco, Costa-Fernández, José Manuel, Ruiz Encinar, Jorge
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Universidad de Cantabria (UC)
Repositorio:UCrea Repositorio Abierto de la Universidad de Cantabria
Idioma:inglés
OAI Identifier:oai:repositorio.unican.es:10902/39484
Acceso en línea:https://hdl.handle.net/10902/39484
Access Level:acceso abierto
Palabra clave:Calibration
Hydrophobicity
Monomers
Peptides and proteins
Sulfur
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spelling Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standardsCid-Barrio, LauraCalderón Celis, FranciscoCosta-Fernández, José ManuelRuiz Encinar, JorgeCalibrationHydrophobicityMonomersPeptides and proteinsSulfurInductively coupled plasma-mass spectrometry (ICP?MS) has been widely used in Life Sciences for the absolute quantification of biomolecules without specific standards, assuming the same response for generic compounds including complex biomolecules. However, contradictory results have been published on this regard. We present the first critical statistical comparison of the ICP-MS response factors obtained for 14 different relevant S-containing biomolecules (three peptides, four proteins, one amino acid, two cofactors, three polyethylene glycol (PEG) derivatives, and sulfate standard), covering a wide range of hydrophobicities and molecular sizes. Two regular flow nebulizers and a total consumption nebulizer (TCN) were tested. ICP?MS response factors were determined though calibration curves, and isotope dilution analysis was used to normalize the results. No statistical differences have been found for low-molecular-weight biocompounds, PEGs, and nonhydrophobic peptides using any of the nebulizers tested. Interestingly, while statistical differences were still found negligible (96-104%) for the proteins and hydrophobic peptide using the TCN, significantly lower response factors (87-40%) were obtained using regular flow nebulizers. Such differential behavior seems to be related mostly to hydrophobicity and partially to the molecular weight. Findings were validated using IDA in intact and digested bovine serum albumin solutions using the TCN (98 and 100%, respectively) and the concentric nebulizer (73 and 97%, respectively). Additionally, in the case of a phosphoprotein, results were corroborated using the P trace in parallel to the S trace used along the manuscript. This work seems to suggest that ICP-MS operated with regular nebulizers can offer absolute quantification using generic standards for most biomolecules except proteins and hydrophobic peptides.Financial support from FC-GRUPIN-ID/2018/000166 (Asturias Regional Government) and CTQ2016–79412-P and PID2019- 109698GBI00 (Ministry of Economy and Competitiveness, Spain) is gratefully acknowledged. Authors want to thank also Agilent for the technical support. LCB acknowledges the Ph.D. grant (FPU15/04989) Spanish Ministry of Education.American Chemical SocietyUniversidad de Cantabria20202020-01-01journal articlehttp://purl.org/coar/resource_type/c_6501NAhttp://purl.org/coar/version/c_be7fb7dd8ff6fe43info:eu-repo/semantics/articlehttps://hdl.handle.net/10902/39484Analytical Chemistry, 2020, 92, 13500-13508reponame:UCrea Repositorio Abierto de la Universidad de Cantabriainstname:Universidad de Cantabria (UC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:repositorio.unican.es:10902/394842026-06-02T12:39:31Z
dc.title.none.fl_str_mv Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
title Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
spellingShingle Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
Cid-Barrio, Laura
Calibration
Hydrophobicity
Monomers
Peptides and proteins
Sulfur
title_short Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
title_full Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
title_fullStr Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
title_full_unstemmed Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
title_sort Assessment of the potential and limitations of elemental mass spectrometry in life sciences for absolute quantification of biomolecules using generic standards
dc.creator.none.fl_str_mv Cid-Barrio, Laura
Calderón Celis, Francisco
Costa-Fernández, José Manuel
Ruiz Encinar, Jorge
author Cid-Barrio, Laura
author_facet Cid-Barrio, Laura
Calderón Celis, Francisco
Costa-Fernández, José Manuel
Ruiz Encinar, Jorge
author_role author
author2 Calderón Celis, Francisco
Costa-Fernández, José Manuel
Ruiz Encinar, Jorge
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidad de Cantabria
dc.subject.none.fl_str_mv Calibration
Hydrophobicity
Monomers
Peptides and proteins
Sulfur
topic Calibration
Hydrophobicity
Monomers
Peptides and proteins
Sulfur
description Inductively coupled plasma-mass spectrometry (ICP?MS) has been widely used in Life Sciences for the absolute quantification of biomolecules without specific standards, assuming the same response for generic compounds including complex biomolecules. However, contradictory results have been published on this regard. We present the first critical statistical comparison of the ICP-MS response factors obtained for 14 different relevant S-containing biomolecules (three peptides, four proteins, one amino acid, two cofactors, three polyethylene glycol (PEG) derivatives, and sulfate standard), covering a wide range of hydrophobicities and molecular sizes. Two regular flow nebulizers and a total consumption nebulizer (TCN) were tested. ICP?MS response factors were determined though calibration curves, and isotope dilution analysis was used to normalize the results. No statistical differences have been found for low-molecular-weight biocompounds, PEGs, and nonhydrophobic peptides using any of the nebulizers tested. Interestingly, while statistical differences were still found negligible (96-104%) for the proteins and hydrophobic peptide using the TCN, significantly lower response factors (87-40%) were obtained using regular flow nebulizers. Such differential behavior seems to be related mostly to hydrophobicity and partially to the molecular weight. Findings were validated using IDA in intact and digested bovine serum albumin solutions using the TCN (98 and 100%, respectively) and the concentric nebulizer (73 and 97%, respectively). Additionally, in the case of a phosphoprotein, results were corroborated using the P trace in parallel to the S trace used along the manuscript. This work seems to suggest that ICP-MS operated with regular nebulizers can offer absolute quantification using generic standards for most biomolecules except proteins and hydrophobic peptides.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
NA
http://purl.org/coar/version/c_be7fb7dd8ff6fe43
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10902/39484
url https://hdl.handle.net/10902/39484
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv Analytical Chemistry, 2020, 92, 13500-13508
reponame:UCrea Repositorio Abierto de la Universidad de Cantabria
instname:Universidad de Cantabria (UC)
instname_str Universidad de Cantabria (UC)
reponame_str UCrea Repositorio Abierto de la Universidad de Cantabria
collection UCrea Repositorio Abierto de la Universidad de Cantabria
repository.name.fl_str_mv
repository.mail.fl_str_mv
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