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An infrared sensor analysing label‐free the secondary structure of the Abeta peptide in presence of complex fluids |
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| Authors: | Andreas Nabers Julian Ollesch Jonas Schartner Carsten Kötting Just Genius Ute Haußmann Hans Klafki Jens Wiltfang Klaus Gerwert |
| Affiliation: | 1. Protein Research Unit Ruhr within Europe (PURE), Ruhr‐University Bochum, Department of Biophysics ND04‐596, Bochum, Germany;2. Protein Research Unit Ruhr within Europe (PURE), LVR‐Hospital Essen, Department of Psychiatry and Psychotherapy, Medical Faculty University of Duisburg‐Essen, Essen, Germany;3. University Medical Center, Department of Psychiatry and Psychotherapy, Georg‐August‐University, G?ttingen, Germany;4. +49 (0)234 32 24461+49 (0)234 32 14238 |
| 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: | Amyloid‐beta neurodegeneration label‐free ATR‐FTIR spectroscopy surface functionalization complex mixture body fluid biosensor |
