Effect of sodium dodecyl sulfate micelles on peptide mass fingerprinting by matrix-assisted laser desorption/ionization mass spectrometry

Rapid Communications in Mass Spectrometry : RCM
Rama Tummala, P A Limbach

Abstract

Here we have examined the effect of sodium dodecyl sulfate (SDS) at various concentrations on matrix-assisted laser desorption/ionization (MALDI) peptide mass fingerprinting experiments. Several model proteins were digested with trypsin and then various amounts of SDS were added prior to MALDI mass spectrometry. Evaluation of the data was made by calculating the amino acid sequence coverage within each analysis. It was found that addition of 0.1-0.3% w/v SDS prior to MALDI analysis results in an increase in the number of tryptic peptides detected thereby improving the total sequence coverage of the analysis. The use of SDS at concentrations near its critical micelle concentration can improve sequence coverage from MALDI peptide mass fingerprinting analyses allowing for increased confidence in protein identification or additional opportunities to identify putative regions of posttranslational modification.

Citations

Nov 18, 2011·Expert Review of Proteomics·Alan A DoucetteShayla Fitzsimmons
Nov 9, 2004·Journal of Mass Spectrometry : JMS
Apr 10, 2010·Journal of Proteome Research·Diane BotelhoAlan Doucette
Jul 13, 2021·Frontiers in Chemistry·Zhenxin WangXinwen Zhou
Aug 10, 2007·Analytical Chemistry·Meiling LiGary R Kinsel
Dec 31, 2005·Analytical Chemistry·Anders NordströmGary Siuzdak

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