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Issue 8, 2005
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Measuring D-amino acid-containing neuropeptides with capillary electrophoresis

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Neuropeptides are heavily posttranslationally modified (PTM) gene products that are often characterized by a variety of mass spectrometric approaches. Recently, the occurrence of amino acids in the D-form has been documented in several neuropeptides. As this modification has no associated mass shift, this particular PTM is difficult to evaluate using mass spectrometry (MS) alone. Here we demonstrate several approaches using capillary electrophoresis (CE) with absorbance and laser-induced fluorescence (LIF) for the separation of native and derivatized molluscan peptides containing D-amino acids. The combination of peptide derivatization followed by CE/LIF is well suited for single cell measurements because of its ability to characterize the peptides in such small samples. In order to verify this approach, the D-Trp-containing peptide NdWFa (NH2-Asn-D-Trp-Phe-CONH2), present in individual neurons from the marine mollusk Aplysia californica, has been characterized. The mass spectra show that NdWFa and/or NWFa are present in specific neurons; CE/LIF analysis of these cells demonstrates that NdWFa is the dominant form of the peptide.

Graphical abstract: Measuring d-amino acid-containing neuropeptides with capillary electrophoresis

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Publication details

The article was received on 13 Apr 2005, accepted on 17 Jun 2005 and first published on 01 Jul 2005

Article type: Paper
DOI: 10.1039/B504717J
Citation: Analyst, 2005,130, 1198-1203
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    Measuring D-amino acid-containing neuropeptides with capillary electrophoresis

    S. A. Sheeley, H. Miao, M. A. Ewing, S. S. Rubakhin and J. V. Sweedler, Analyst, 2005, 130, 1198
    DOI: 10.1039/B504717J

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