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Abstract

The removal of sodium dodecyl sulfate (SDS) in SDS-assisted proteomics with electrospray-ionization-mass-spectrometric (ESI-MS) analysis is an essential step in the analysis. Off-line state-of-the-art sample-preparation strategies can allow 100% removal of DS- and up to 100% peptide recoveries. These strategies, however, are typically laborious and require long analysis times and a complex experimental setup. Here, we developed a simple, membrane-free, electrokinetic, on-line, integrated SDS removal–ESI-MS device that was able to enhance ESI-MS signals of bradykinin and peptides from trypsin-digested bovine serum albumin (BSA) in samples that contained SDS micelles. The significant peptide-signal improvements were contributed by the complete removal of DS- and the enrichment of the peptides in the presence of an electric field. Enrichment was via micelle-to-solvent stacking, initially developed in capillary electrophoresis. Bradykinin percent recovery was 800%, and BSA peptide percent recovery was 87%. Enhancement factors in ESI-MS signals (after and before removal) for selected m/z values of peptides from the BSA digest were 535-693.

Item Type:	Article
Authors/Creators:	Tubaon, RM and Haddad, PR and Quirino, JP
Keywords:	mass spectrometry, sample preparation
Journal or Publication Title:	Analytical Chemistry
Publisher:	Amer Chemical Soc
ISSN:	0003-2700
DOI / ID Number:	10.1021/acs.analchem.8b01707
Copyright Information:	Copyright 2018 American Chemical Society
Related URLs:	UTAS Profile: Tubaon, RM UTAS Profile: Haddad, PR Google Scholar: Quirino, JP UTAS Profile: Quirino, JP
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