TY - JOUR
T1 - Quantitative Label-Free Single-Cell Proteomics on the Orbitrap Astral MS
AU - Petrosius, Valdemaras
AU - Aragon-Fernandez, Pedro
AU - Arrey, Tabiwang N
AU - Woessman, Jakob
AU - Üresin, Nil
AU - de Boer, Bauke
AU - Su, Jinyu
AU - Furtwängler, Benjamin
AU - Stewart, Hamish
AU - Denisov, Eduard
AU - Petzoldt, Johannes
AU - Peterson, Amelia C
AU - Hock, Christian
AU - Damoc, Eugen
AU - Makarov, Alexander
AU - Zabrouskov, Vlad
AU - Porse, Bo T
AU - Schoof, Erwin M
N1 - Copyright © 2025 The Authors. Published by Elsevier Inc. All rights reserved.
PY - 2025/5/5
Y1 - 2025/5/5
N2 - Single-cell proteomics by mass spectrometry (scp-MS) holds the potential to provide unprecedented insights into molecular features directly linked to the cellular phenotype while deconvoluting complex organisms into their basic building blocks. Tailored sample preparation that maximizes the extracted amount of material that is introduced into the mass spectrometer has rapidly propelled the field forward. However, the measured signal is still at the lower edge of detection, approaching the sensitivity boundary of current instrumentation. Here, we investigate the capacity of the enhanced sensitivity of the Orbitrap Astral mass spectrometer to facilitate deeper proteome profiles from low-input to single-cell samples. We carry out a comprehensive data acquisition method survey to pinpoint which parameters provide the most sensitivity. Furthermore, we explore the quantitative accuracy of the obtained measurements to ensure that the obtained abundances are in line with expected ground truth values. We culminate our technical exploration by generating small datasets from two cultured cell lines and a primary bone marrow sample, to showcase obtainable proteome coverage differences from different source materials. Finally, as a proof of concept, we explore protein covariation to showcase how information on known protein complexes is captured inherently in our scp-MS data.
AB - Single-cell proteomics by mass spectrometry (scp-MS) holds the potential to provide unprecedented insights into molecular features directly linked to the cellular phenotype while deconvoluting complex organisms into their basic building blocks. Tailored sample preparation that maximizes the extracted amount of material that is introduced into the mass spectrometer has rapidly propelled the field forward. However, the measured signal is still at the lower edge of detection, approaching the sensitivity boundary of current instrumentation. Here, we investigate the capacity of the enhanced sensitivity of the Orbitrap Astral mass spectrometer to facilitate deeper proteome profiles from low-input to single-cell samples. We carry out a comprehensive data acquisition method survey to pinpoint which parameters provide the most sensitivity. Furthermore, we explore the quantitative accuracy of the obtained measurements to ensure that the obtained abundances are in line with expected ground truth values. We culminate our technical exploration by generating small datasets from two cultured cell lines and a primary bone marrow sample, to showcase obtainable proteome coverage differences from different source materials. Finally, as a proof of concept, we explore protein covariation to showcase how information on known protein complexes is captured inherently in our scp-MS data.
UR - http://www.scopus.com/inward/record.url?scp=105010576008&partnerID=8YFLogxK
U2 - 10.1016/j.mcpro.2025.100982
DO - 10.1016/j.mcpro.2025.100982
M3 - Journal article
C2 - 40334743
SN - 1535-9484
VL - 24
JO - Molecular & Cellular Proteomics
JF - Molecular & Cellular Proteomics
IS - 6
M1 - 100982
ER -