Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins
[Image: see text] We describe an instrument configuration based on the Orbitrap Exploris 480 mass spectrometer that has been coupled to an Omnitrap platform. The Omnitrap possesses three distinct ion-activation regions that can be used to perform resonant-based collision-induced dissociation, severa...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10433246/ https://www.ncbi.nlm.nih.gov/pubmed/37534599 http://dx.doi.org/10.1021/acs.analchem.3c01899 |
_version_ | 1785091608103878656 |
---|---|
author | Smyrnakis, Athanasios Levin, Nikita Kosmopoulou, Mariangela Jha, Ajay Fort, Kyle Makarov, Alexander Papanastasiou, Dimitris Mohammed, Shabaz |
author_facet | Smyrnakis, Athanasios Levin, Nikita Kosmopoulou, Mariangela Jha, Ajay Fort, Kyle Makarov, Alexander Papanastasiou, Dimitris Mohammed, Shabaz |
author_sort | Smyrnakis, Athanasios |
collection | PubMed |
description | [Image: see text] We describe an instrument configuration based on the Orbitrap Exploris 480 mass spectrometer that has been coupled to an Omnitrap platform. The Omnitrap possesses three distinct ion-activation regions that can be used to perform resonant-based collision-induced dissociation, several forms of electron-associated fragmentation, and ultraviolet photodissociation. Each section can also be combined with infrared multiphoton dissociation. In this work, we demonstrate all these modes of operation in a range of peptides and proteins. The results show that this instrument configuration produces similar data to previous implementations of each activation technique and at similar efficiency levels. We demonstrate that this unique instrument configuration is extremely versatile for the investigation of polypeptides. |
format | Online Article Text |
id | pubmed-10433246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-104332462023-08-18 Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins Smyrnakis, Athanasios Levin, Nikita Kosmopoulou, Mariangela Jha, Ajay Fort, Kyle Makarov, Alexander Papanastasiou, Dimitris Mohammed, Shabaz Anal Chem [Image: see text] We describe an instrument configuration based on the Orbitrap Exploris 480 mass spectrometer that has been coupled to an Omnitrap platform. The Omnitrap possesses three distinct ion-activation regions that can be used to perform resonant-based collision-induced dissociation, several forms of electron-associated fragmentation, and ultraviolet photodissociation. Each section can also be combined with infrared multiphoton dissociation. In this work, we demonstrate all these modes of operation in a range of peptides and proteins. The results show that this instrument configuration produces similar data to previous implementations of each activation technique and at similar efficiency levels. We demonstrate that this unique instrument configuration is extremely versatile for the investigation of polypeptides. American Chemical Society 2023-08-03 /pmc/articles/PMC10433246/ /pubmed/37534599 http://dx.doi.org/10.1021/acs.analchem.3c01899 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Smyrnakis, Athanasios Levin, Nikita Kosmopoulou, Mariangela Jha, Ajay Fort, Kyle Makarov, Alexander Papanastasiou, Dimitris Mohammed, Shabaz Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins |
title | Characterization
of an Omnitrap-Orbitrap Platform
Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation,
and Electron Capture Dissociation for the Analysis of Peptides and
Proteins |
title_full | Characterization
of an Omnitrap-Orbitrap Platform
Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation,
and Electron Capture Dissociation for the Analysis of Peptides and
Proteins |
title_fullStr | Characterization
of an Omnitrap-Orbitrap Platform
Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation,
and Electron Capture Dissociation for the Analysis of Peptides and
Proteins |
title_full_unstemmed | Characterization
of an Omnitrap-Orbitrap Platform
Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation,
and Electron Capture Dissociation for the Analysis of Peptides and
Proteins |
title_short | Characterization
of an Omnitrap-Orbitrap Platform
Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation,
and Electron Capture Dissociation for the Analysis of Peptides and
Proteins |
title_sort | characterization
of an omnitrap-orbitrap platform
equipped with infrared multiphoton dissociation, ultraviolet photodissociation,
and electron capture dissociation for the analysis of peptides and
proteins |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10433246/ https://www.ncbi.nlm.nih.gov/pubmed/37534599 http://dx.doi.org/10.1021/acs.analchem.3c01899 |
work_keys_str_mv | AT smyrnakisathanasios characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT levinnikita characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT kosmopouloumariangela characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT jhaajay characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT fortkyle characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT makarovalexander characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT papanastasioudimitris characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins AT mohammedshabaz characterizationofanomnitraporbitrapplatformequippedwithinfraredmultiphotondissociationultravioletphotodissociationandelectroncapturedissociationfortheanalysisofpeptidesandproteins |