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Briefings in Functional Genomics and Proteomics Advance Access originally published online on June 20, 2007
Briefings in Functional Genomics and Proteomics 2007 6(2):149-158; doi:10.1093/bfgp/elm010
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© Oxford University Press, 2007, All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Quantitative analysis of amyloid-ß peptides in cerebrospinal fluid using immunoprecipitation and MALDI-Tof mass spectrometry

Valentina Gelfanova, Richard E. Higgs, Robert A. Dean, David M. Holtzman, Martin R. Farlow, Eric R. Siemers, Amechand Boodhoo, Yue-Wei Qian, Xiaohua He, Zhaoyan Jin, Deborah L. Fisher, Karen L. Cox and John E. Hale

Corresponding author. John E. Hale, Lilly Research Laboratories, P.O. Box 708, Greenfield, IN 46140, USA. E-mail: hale_john_E{at}lilly.com

Immunoprecipitation (IP) combined with matrix-assisted laser desorption ionization (MALDI) time of flight (Tof) mass spectrometry has been used to develop quantitative assays for amyloid-ß (Aß) peptides in cerebrospinal fluid (CSF). Inclusion of 15N labelled standard peptides allows for absolute quantification of multiple Aß isoforms in individual samples. Characterization of variability associated with all steps of the assay indicated that the IP step is the single largest contributor to overall variability. Optimization of the assay resulted in overall coefficient of variation ≤8% with high agreement to an Aß1-40 and Aß1-42 ELISA assay. Application of the MALDI-Tof assay to CSF obtained from healthy volunteers and Alzheimer's disease patients indicated statistically significant 43% lower levels of Aß1-42 in the AD group (P = 0.0025).

Keywords: Alzheimers disease, amyloid-ß peptide, MALDI-Tof mass spectrometry, multiplexed analysis


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