Using surface-assisted laser desorption/ionization mass spectrometry to detect proteins and protein-protein complexes

Wen Tsen Chen, Cheng Kang Chiang, Chia Hsin Lee, Huan Tsung Chang*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

23 Scopus citations

Abstract

In this study, we combined surface-assisted laser desorption/ ionization mass spectrometry (SALDI-MS) with HgTe nanostructures as matrix for the detection of several proteins (á1-antitrypsin, trypsin, IgG, protein G) and their complexes. We investigated the effects of several parameters (the concentration and nature of surfactants and metal ions, the pH, and concentration of the analytes in the sample matrixes) on the sensitivity of the detection of these proteins and their complexes. The presence of stabilizing Brij 76 surfactant and Zn(II) ions allowed the detection of weak protein complexes, such as á1-antitrypsin.trypsin and IgG.protein G complexes, at the picomole level. We observed multiply charged states at m/z 72 160 ([α1- antitrypsin + trypsin + H] +) and 86 585 ([IgG + protein G + 2H] 2+) for the α1- antitrypsin.trypsin and IgG.protein G complexes, respectively. To the best of our knowledge, detection of weak protein complexes and determination of their stoichiometry have not been demonstrated previously when a combination of SALDI-MS and nanostructures were used. This simple and reproducible SALDI-MS approach using HgTe nanostructures holds great potential for the detection of other proteins and their complexes.

Original languageEnglish
Pages (from-to)1924-1930
Number of pages7
JournalAnalytical Chemistry
Volume84
Issue number4
DOIs
StatePublished - 21 02 2012
Externally publishedYes

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