Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00636226" target="_blank" >RIV/61388963:_____/25:00636226 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10510119

Výsledek na webu

<a href="https://doi.org/10.1021/jasms.5c00037" target="_blank" >https://doi.org/10.1021/jasms.5c00037</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jasms.5c00037" target="_blank" >10.1021/jasms.5c00037</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry

Popis výsledku v původním jazyce

Bottom-up proteomics typically involves enzymatic digestion of proteins, generating a complex peptide mixture. These peptides are separated using reversed-phase ultrahigh-performance liquid chromatography (UHPLC) and analyzed using electrospray ionization (ESI) tandem mass spectrometry (MS/MS) in positive ion mode. Despite its widespread use, this approach has limitations, particularly in ionizing highly acidic or hydrophobic peptides and detecting certain post-translational modifications (PTMs). To overcome these challenges, alternative ionization methods, such as vacuum ultraviolet (VUV) atmospheric pressure photoionization (APPI), have been explored. In this study, we propose peptide analysis using a novel prototype APPI source employing soft X-ray photons. Soft X-ray photons possess orders of magnitude higher energy than VUV photons, enabling additional ionization pathways. Here, we present peptide ionization data using soft X-ray and VUV APPI in both positive and negative ion modes. Notably, soft X-ray photons exhibited a remarkable capacity to generate deprotonated peptides and hydrogen-deficient peptide radical anions ([M – 2H]•–), outperforming conventional VUV photons. Furthermore, collision-induced dissociation (CID) of [M – 2H]•– provided unique structural insight, facilitating PTM characterization. Our findings emphasize the significant potential of soft X-ray APPI in advancing peptide analysis and highlight the utility of negative ion mode for proteomic applications.

Název v anglickém jazyce

Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry

Popis výsledku anglicky

Bottom-up proteomics typically involves enzymatic digestion of proteins, generating a complex peptide mixture. These peptides are separated using reversed-phase ultrahigh-performance liquid chromatography (UHPLC) and analyzed using electrospray ionization (ESI) tandem mass spectrometry (MS/MS) in positive ion mode. Despite its widespread use, this approach has limitations, particularly in ionizing highly acidic or hydrophobic peptides and detecting certain post-translational modifications (PTMs). To overcome these challenges, alternative ionization methods, such as vacuum ultraviolet (VUV) atmospheric pressure photoionization (APPI), have been explored. In this study, we propose peptide analysis using a novel prototype APPI source employing soft X-ray photons. Soft X-ray photons possess orders of magnitude higher energy than VUV photons, enabling additional ionization pathways. Here, we present peptide ionization data using soft X-ray and VUV APPI in both positive and negative ion modes. Notably, soft X-ray photons exhibited a remarkable capacity to generate deprotonated peptides and hydrogen-deficient peptide radical anions ([M – 2H]•–), outperforming conventional VUV photons. Furthermore, collision-induced dissociation (CID) of [M – 2H]•– provided unique structural insight, facilitating PTM characterization. Our findings emphasize the significant potential of soft X-ray APPI in advancing peptide analysis and highlight the utility of negative ion mode for proteomic applications.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

<a href="/cs/project/GA20-09126S" target="_blank" >GA20-09126S: Využití ionizací v plynné fázi za atmosferického tlaku pro hmotnostní spektrometrii peptidů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of the American Society for Mass Spectrometry

ISSN

1044-0305

e-ISSN

1879-1123

Svazek periodika

36

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1286-1295

Kód UT WoS článku

001491168900001

EID výsledku v databázi Scopus

2-s2.0-105005499480