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Direct antigen detection from immunoprecipitated beads using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry; a new method for immunobeads‐mass spectrometry (iMS)
Author(s) -
Shimada Takashi,
Toyama Atsuhiko,
Aoki Chikage,
Aoki Yutaka,
Tanaka Koichi,
Sato TakaAki
Publication year - 2011
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.5259
Subject(s) - chemistry , mass spectrometry , chromatography , matrix assisted laser desorption/ionization , capillary electrophoresis–mass spectrometry , time of flight mass spectrometry , matrix (chemical analysis) , immunoprecipitation , ionization , desorption , electrospray ionization , biochemistry , ion , organic chemistry , adsorption , gene
One‐step detection of biological molecules is one of the principal techniques for clinical diagnosis, and the potential of mass spectrometry for biomarker detection has been a promising new approach in the field of medical sciences. We demonstrate here a new and high‐sensitivity method that we termed immunobeads‐mass spectrometry (iMS), which combines conventional immunoprecipitation and matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOF MS). The key feature of iMS is the MS‐compatible condition of immunoprecipitation using detergents with a monosaccaride‐C8 alkyl chain or a disaccharide‐C10 alkyl chain, and the minimized number of steps required for high‐sensitivity detection of target peptides in serum or biological fluid. This was achieved by optimizing the wash buffer and subjecting the immunobeads directly to MALDI‐TOF MS analysis. Using this method, we showed that 1 fmol of amyloid beta peptide spiked in serum was readily detectable, demonstrating the powerful tool of iMS as a biomarker detection method. Copyright © 2011 John Wiley & Sons, Ltd.