Quantitation of Amyloid Beta Peptides in CSF by Surface Enhanced MALDI-TOF

  • Eddie Takahashi
  • Anita Howe
  • Ole Vesterqvist
  • Zhaosheng Lin
Part of the Methods in Molecular Biology book series (MIMB, volume 818)

Abstract

Alzheimer’s disease is characterized by the deposition of amyloid plaques in the brain. The major components of these plaques are β-amyloid (Aβ) peptides. The CSF concentration of these peptides can therefore provide a valuable biomarker for potentially predicting the state of disease and/or monitoring the efficacy of a drug aiming to inhibit the formation of amyloid plaques. Although the concentration of a given peptide in CSF can easily be measured by ELISA methods, few methods are able to simultaneously observe and distinguish between various peptides of similar yet slightly different amino acid composition. The Surface Enhanced Laser Desorption/Ionization–Time Of Flight mass spectrometry (SELDI-TOF) technology, a platform combining the use of an antibody and MALDI-TOF, can be used to simultaneously detect and quantitate various Aβ peptides with sensitivities in the picomolar range.

Key words

β-Amyloid peptides Aβ40 Aβ42 Alzheimer’s disease MALDI-TOF SELDI-TOF CSF Quantitation 

Notes

Acknowledgments

The authors would like to thank Dr. Amanda Bulman for her constructive suggestions and SELDI-related technical support throughout the development of this method.

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Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Eddie Takahashi
    • 1
  • Anita Howe
    • 1
  • Ole Vesterqvist
    • 1
  • Zhaosheng Lin
    • 1
  1. 1.Wyeth ResearchCollegevilleUSA

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