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...

Descripción completa

Detalles Bibliográficos
Autores principales: Smyrnakis, Athanasios, Levin, Nikita, Kosmopoulou, Mariangela, Jha, Ajay, Fort, Kyle, Makarov, Alexander, Papanastasiou, Dimitris, Mohammed, Shabaz
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