Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/139188
Title: Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
Authors: Serra, Aida
Gallart-Palau, Xavier
Dutta, Bamaprasad
Sze, Siu Kwan
Keywords: Science::Biological sciences
Issue Date: 2018
Source: Serra, A., Gallart-Palau, X., Dutta, B., & Sze, S. K. (2018). Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics. Journal of proteome research, 17(7), 2390-2400. doi:10.1021/acs.jproteome.8b00156
Journal: Journal of proteome research
Abstract: Biological research often requires the use of sodium dodecyl sulfate (SDS) to solubilize protein samples; however, this detergent is not compatible with direct mass spectrometry (MS) analysis. Here, we report an online high-throughput proteomics method that permits standard in-solution digestion of SDS-containing samples followed by direct liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) analysis using weak cation-exchange chromatography (WCX). This approach, called the online removal of sodium dodecyl sulfate (Online reSDS), exploits the properties of WCX in a highly organic and mildly acidic medium to retain positively charged peptides by both hydrophilic interaction and electrostatic attraction while simultaneously repelling negative SDS molecules. This method was optimized to successfully analyze complex samples that contain up to 1% of SDS. Furthermore, online reSDS improves the identification of peptides with post-translational modifications (PTMs), such as deamidation and phosphorylation, without preliminary enrichment. In conclusion, we show that reSDS can facilitate research in proteomics by allowing the use of SDS in a wide range of LC-MS/MS applications with simplified sample-processing procedures.
URI: https://hdl.handle.net/10356/139188
ISSN: 2193-5807
DOI: 10.1021/acs.jproteome.8b00156
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of proteome research, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jproteome.8b00156
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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