An infrared sensor analysing label-free the secondary structure of the Abeta peptide in presence of complex fluids

J Biophotonics. 2016 Mar;9(3):224-34. doi: 10.1002/jbio.201400145. Epub 2015 Mar 23.

Abstract

The secondary structure change of the Abeta peptide to beta-sheet was proposed as an early event in Alzheimer's disease. The transition may be used for diagnostics of this disease in an early state. We present an Attenuated Total Reflection (ATR) sensor modified with a specific antibody to extract minute amounts of Abeta peptide out of a complex fluid. Thereby, the Abeta peptide secondary structure was determined in its physiological aqueous environment by FTIR-difference-spectroscopy. The presented results open the door for label-free Alzheimer diagnostics in cerebrospinal fluid or blood. It can be extended to further neurodegenerative diseases. An immunologic ATR-FTIR sensor for Abeta peptide secondary structure analysis in complex fluids is presented.

Keywords: ATR-FTIR spectroscopy; Amyloid-beta; biosensor; body fluid; complex mixture; label-free; neurodegeneration; surface functionalization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Animals
  • Biomimetics
  • Chick Embryo
  • Models, Molecular
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared / instrumentation*
  • Water / chemistry*

Substances

  • Amyloid beta-Peptides
  • Water