Evidence map›Paper›PMID 38363304›Full record

ArticleAnalytical and bioanalytical chemistry2024

Evaluation of different isotope dilution mass spectrometry strategies for the characterization of naturally abundant and isotopically labelled peptide standards.

Jesús Nicolás Carcelén, Helí Potes Rodríguez, Adriana González-Gago, Juan Manuel Marchante-Gayón, Alfredo Ballesteros, José Manuel González, José Ignacio García Alonso, Pablo Rodríguez-González

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In one paragraph

Article in Analytical and bioanalytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 45% of its field
1 · What the graph read from it

What it found

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 2 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Jesús Nicolás CarcelénDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Helí Potes RodríguezDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Adriana González-GagoDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Juan Manuel Marchante-GayónDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain. marchant@uniovi.es.
Alfredo BallesterosDepartment of Organic and Inorganic Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
José Manuel GonzálezDepartment of Organic and Inorganic Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
José Ignacio García AlonsoDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Pablo Rodríguez-GonzálezDepartment of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Universidad de Oviedo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural abundance and isotopically labelled tryptic peptides are routinely employed as standards in quantitative proteomics. The certification of the peptide content is usually carried out by amino acid analysis using isotope dilution mass spectrometry (IDMS) after the acid hydrolysis of the peptide. For the validation and traceability of the amino acid analysis procedure, expensive certified peptides must be employed. In this work we evaluate different IDMS alternatives which will reduce the amount of certified peptide required for validation of the amino acid analysis procedure. In this context, the characterization of both natural and isotopically labelled synthetic angiotensin I peptides was carried out. First, we applied a fast procedure for peptide hydrolysis based on microwave-assisted digestion and employed two certified peptide reference materials SRM 998 angiotensin I and CRM 6901-b C-peptide for validation of the hydrolysis procedure. The amino acids proline, leucine, isoleucine, valine, tyrosine, arginine and phenylalanine were evaluated for their suitability for peptide certification by IDMS by both liquid chromatography with tandem mass spectrometry (LC-MS/MS) and gas chromatography with mass spectrometry (GC)-MS/MS. Then, natural angiotensin I and

Indexed as

Angiotensin ITandem Mass SpectrometryAmino AcidsChromatography, LiquidGas Chromatography-Mass SpectrometryIsotopesPeptidesReference StandardsAmino AcidsAngiotensin IIsotopesPeptidesIsotope dilution analysisMass spectrometryPeptide characterization

Identifiers

PMID38363304
PMCPMC10899365
OpenAlexW4391881246

What OpenQuestion holds

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LicenceCC BY
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.