Nα Selective Acetylation of Peptides

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 gro...

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Bibliographic Details
Published in:Mass Spectrometry 2012, Vol.1(2), pp.A0010-A0010
Main Authors: Mikami, Toshiyuki, Takao, Toshifumi, Yanagi, Kazunori, Nakazawa, Hiroshi
Format: Article
Language:English
Subjects:
acetylation
isotope-labeling
Original
peptide
protein
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Summary: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.
ISSN:2187-137X
2186-5116
DOI:10.5702/massspectrometry.A0010