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Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation

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Journal of the American Society for Mass Spectrometry

Abstract

The complexation between an 18-residue zinc finger peptide of CCHC type (CCHC=Cys-X2-Cys-X4-His-X4-Cys, X=variable amino acid) from the gag protein p55 of human immunodeficiency virus type 1 (HIV-1) and various transition metal ions was studied by means of circular dichroism spectroscopy and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). A correlation between the complexation behavior in solution and in MALDI-MS could be established. It was shown that MALDI-MS is a fast method suitable for studying metal binding properties of zinc finger complexes.

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Authors and Affiliations

  1. Laboratory of Organic Chemistry, ETH Zürich, Zürich, Switzerland

    Edda Lehmann & Renato Zenobi

  2. Laboratory of Biochemistry, ETH Zürich, Zürich, Switzerland

    Stefan Vetter

Authors
  1. Edda Lehmann
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  2. Renato Zenobi
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  3. Stefan Vetter
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Correspondence to Renato Zenobi.

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Lehmann, E., Zenobi, R. & Vetter, S. Matrix-assisted laser desorption/ionization mass spectra reflect solution-phase zinc finger peptide complexation. J Am Soc Mass Spectrom 10, 27–34 (1999). https://doi.org/10.1016/S1044-0305(98)00116-0

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  • DOI: https://doi.org/10.1016/S1044-0305(98)00116-0

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