Binding of alpha 1-acid glycoprotein with aconitum alkaloids: an investigation using an intensity fading matrix-assisted laser desorption/ionization Fourier transform mass spectrometry method

Authors

  • Wenlong Liu,

    1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
    2. Graduate School of the Chinese Academy of Sciences, Beijing, P.R. China
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  • Shu Liu,

    1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
    2. Graduate School of the Chinese Academy of Sciences, Beijing, P.R. China
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  • Huilin Li,

    1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
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  • Fengrui Song,

    1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
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  • Zhiqiang Liu,

    1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
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  • Shuying Liu

    Corresponding author
    • Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P.R. China
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S. Y. Liu, Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 5625 Renmin Street, Changchun 130022, P.R. China.

E-mail: syliu19@yahoo.com.cn

Abstract

Intensity fading matrix-assisted laser desorption/ionization (IF-MALDI) mass spectrometry has become an alternative screening approach for the affinity-binding analysis of proteins and peptides with ligands. In this study, an attempt has been made to study the interaction of alpha 1-acid glycoprotein (AGP) with aconitum alkaloids by IF-MALDI Fourier transform ion cyclotron resonance mass spectrometry (IF-MALDI-FT-MS). Compared with the nonbinding internal standard, clear reduction in the ion abundances of the target alkaloids was observed with the addition of AGP. Relative binding affinities of different alkaloids towards the protein could also be estimated using IF-MALDI-FT-MS. The binding affinity was also investigated by using ultrafiltration liquid chromatography with photodiode array detection coupled to electrospray ionization mass spectrometry (ultrafiltration LC-DAD/ESI-MS), and results were consistent with that of IF-MALDI-FT-MS. Copyright © 2011 John Wiley & Sons, Ltd.

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