Diagonal chromatographic selection of cysteinyl peptides modified with benzoquinones |
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Authors: | Loïc Dayon Hubert H Girault |
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Institution: | (1) Laboratoire d’Electrochimie Physique et Analytique, Ecole Polytechnique Fédérale de Lausanne (EPFL), Station 6, 1015 Lausanne, Switzerland;(2) Present address: Biomedical Proteomics Research Group, Department of Structural Biology and Bioinformatics, Faculty of Medicine, University of Geneva, Geneva, Switzerland |
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Abstract: | The derivatization of cysteine-containing peptides with benzoquinone compounds is rapid, quantitative and specific in acidic
media. The conversion of cysteines into hydrophobic benzoquinone-adducted residues in peptides is used here to alter the chromatographic
properties of cysteinyl peptides during liquid chromatography separation. The benzoquinone derivatization is shown to allow
the accurate selection of cysteine-containing peptides of bovine serum albumin tryptic digest by diagonal reversed-phase chromatography,
which consists of one primary and a series of secondary identical liquid chromatographic separations, before and after a cysteinyl-targeted
modification of the peptides by benzoquinone compounds.
Figure Diagonal chromatographic selection of cysteinyl peptides modified with benzoquinones
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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Keywords: | COFRADIC™ Labeling Liquid chromatography Mass spectrometry Proteomics Tagging |
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