Nα Selective Acetylation of Peptides

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概要

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• A chemical tag at the peptide N-terminus, in combination with MS, can be useful for quantitative analysis, N-terminal peptide identification, or peptide sequencing. Here we report on the Nα selective acetylation of a peptide using acetic anhydride, a popular reagent for the modification of amino groups, without the need for the blocking of lysine side-chain ε-amino groups, which is usually required for Nα selective acetylation. By controlling the amount of acetic anhydride used and running the reaction at 0°C, it is possible to preferentially acetylate the α-amino group. As a typical application of the method, a tryptic digest of an N-terminally blocked protein, cytochrome c, was directly acetylated using the present method. When deuterated acetic anhydride was used as the reagent, the N-terminal blocked peptide could be easily identified as a non-labeled ion peak while the Nα-acetyl groups of all the other peptides were deuterated.

著者

• Takao Toshifumi

  Laboratory Of Protein Profiling And Functional Proteomics Institute For Protein Research Osaka Unive

• Yanagi Kazunori

  Genomic Science Laboratories, Dainippon Sumitomo Pharma Co., Ltd.

• Mikami Toshiyuki

  Genomic Science Laboratories, Dainippon Sumitomo Pharma Co., Ltd.

• Nakazawa Hiroshi

  Pharmaceutical Business Division, Sumika Chemical Analysis Service, Ltd.

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