Efficient in-gel digestion procedure using 5-cyclohexyl-1-pentyl-beta-D-maltoside as an additive for gel-based membrane proteomics

Rapid Commun Mass Spectrom. 2004;18(20):2388-94. doi: 10.1002/rcm.1637.

Abstract

A cycloalkyl aliphatic saccharide, 5-cyclohexyl-1-pentyl-beta-D-maltoside (CYMAL-5), was evaluated as a novel additive in a high-throughput in-gel protein digestion system using 96-well plates. Addition of 0.1% CYMAL-5 (final concentration) during trypsin treatment was compatible with both matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and liquid chromatography/tandem mass spectrometry (LC/MS/MS) analysis, and gave a better digestion efficiency than n-octylglucoside, which we previously reported. In-gel reduction and alkylation of Cys residues under denaturing conditions also improved the sequence coverage of peptides. In-gel tryptic digestion with the optimum combination of 0.5 mm thick gels, negative staining, alkylation under denaturing conditions (6 M guanidine hydrochloride), and digestion in the presence of CYMAL-5, gave excellent performance especially for membrane protein analysis, where recovery of hydrophobic peptides was markedly enhanced. The new protocol is simple and convenient, and should be widely applicable to gel-based proteomics.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Alkylation
  • Bacteriorhodopsins / analysis
  • Bacteriorhodopsins / chemistry
  • Bacteriorhodopsins / isolation & purification
  • Cell Line, Tumor
  • Chemical Fractionation / methods*
  • Chromatography, High Pressure Liquid / methods*
  • Colonic Neoplasms / metabolism*
  • Gels / chemistry
  • Glucosides / chemistry*
  • Humans
  • Membrane Proteins / analysis
  • Membrane Proteins / chemistry*
  • Membrane Proteins / isolation & purification*
  • Neoplasm Proteins / analysis
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / isolation & purification
  • Phospholipases A / analysis
  • Phospholipases A / chemistry
  • Phospholipases A / isolation & purification
  • Proteomics / methods
  • Spectrometry, Mass, Electrospray Ionization / methods
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
  • Trypsin / chemistry

Substances

  • Gels
  • Glucosides
  • Membrane Proteins
  • Neoplasm Proteins
  • cyclohexyl-pentyl-maltoside
  • Bacteriorhodopsins
  • Phospholipases A
  • Trypsin