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

Result code in 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>

Alternative codes found

RIV/00216208:11310/25:10510119

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10406 - Analytical chemistry

Project

<a href="/en/project/GA20-09126S" target="_blank" >GA20-09126S: The utility of atmospheric pressure gas-phase ionizations in mass spectrometry of peptides</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

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

Name of the periodical

Journal of the American Society for Mass Spectrometry

ISSN

1044-0305

e-ISSN

1879-1123

Volume of the periodical

36

Issue of the periodical within the volume

6

Country of publishing house

US - UNITED STATES

Number of pages

10

Pages from-to

1286-1295

UT code for WoS article

001491168900001

EID of the result in the Scopus database

2-s2.0-105005499480