SynchroSep-MS: Parallel LC Separations for Multiplexed Proteomics.
Saved in:
| Title: | SynchroSep-MS: Parallel LC Separations for Multiplexed Proteomics. |
|---|---|
| Authors: | Lancaster, Noah M.1,2 (AUTHOR), Chen, Li-Yu1,2 (AUTHOR), Zhao, Bingnan2 (AUTHOR), Anderson, Benton J.2 (AUTHOR), Probasco, Mitchell D.2,3 (AUTHOR), Demichev, Vadim4 (AUTHOR), Polasky, Daniel A.5 (AUTHOR), Nesvizhskii, Alexey I.5,6 (AUTHOR), Overmyer, Katherine A.2,3,7 (AUTHOR), Quarmby, Scott T.2,7 (AUTHOR), Coon, Joshua J.1,2,3,7 (AUTHOR) coon@wisc.edu |
| Source: | Journal of the American Society for Mass Spectrometry. 9/3/2025, Vol. 36 Issue 9, p1979-1987. 9p. |
| Abstract: | Achieving high throughput remains a challenge in MS-based proteomics for large-scale applications. We introduce SynchroSep-MS, a novel method for parallelized, label-free proteome analysis that leverages the rapid acquisition speed of modern mass spectrometers. This approach employs multiple liquid chromatography columns, each with an independent sample, simultaneously introduced into a single mass spectrometer inlet. A precisely controlled retention time offset between sample injections creates distinct elution profiles, facilitating unambiguous analyte assignment. We modified the DIA-NN workflow to effectively process these unique parallelized data, accounting for retention time offsets. Using a dual-column setup with mouse brain peptides, SynchroSep-MS detected approximately 16,700 unique protein groups, nearly doubling the peptide information obtained from a conventional single proteome analysis. The method demonstrated excellent precision and reproducibility (median protein %RSDs less than 4%) and high quantitative linearity (median R2 greater than 0.96) with minimal matrix interference. SynchroSep-MS represents a new paradigm for data collection and the first example of label-free multiplexed proteome analysis via parallel LC separations, offering a direct strategy to accelerate throughput for demanding applications such as large-scale clinical cohorts and single-cell analyses without compromising peak capacity or causing ionization suppression. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
Be the first to leave a comment!