Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics

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...

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Main Authors: Serra, Aida, Gallart-Palau, Xavier, Dutta, Bamaprasad, Sze, Siu Kwan
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2020
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Online Access:https://hdl.handle.net/10356/139188
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1391882023-02-28T17:10:25Z Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics Serra, Aida Gallart-Palau, Xavier Dutta, Bamaprasad Sze, Siu Kwan School of Biological Sciences Science::Biological sciences Sodium Dodecyl Sulfate Weak Cation Exchange 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. MOE (Min. of Education, S’pore) NMRC (Natl Medical Research Council, S’pore) Accepted version 2020-05-18T02:47:07Z 2020-05-18T02:47:07Z 2018 Journal Article 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 2193-5807 https://hdl.handle.net/10356/139188 10.1021/acs.jproteome.8b00156 29888605 2-s2.0-85048711654 7 17 2390 2400 en Journal of proteome research 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 application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences
Sodium Dodecyl Sulfate
Weak Cation Exchange
spellingShingle Science::Biological sciences
Sodium Dodecyl Sulfate
Weak Cation Exchange
Serra, Aida
Gallart-Palau, Xavier
Dutta, Bamaprasad
Sze, Siu Kwan
Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Serra, Aida
Gallart-Palau, Xavier
Dutta, Bamaprasad
Sze, Siu Kwan
format Article
author Serra, Aida
Gallart-Palau, Xavier
Dutta, Bamaprasad
Sze, Siu Kwan
author_sort Serra, Aida
title Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
title_short Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
title_full Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
title_fullStr Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
title_full_unstemmed Online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
title_sort online removal of sodium dodecyl sulfate via weak cation exchange in liquid chromatography-mass spectrometry based proteomics
publishDate 2020
url https://hdl.handle.net/10356/139188
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