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An infrared sensor analysing label‐free the secondary structure of the Abeta peptide in presence of complex fluids
Author(s) -
Nabers Andreas,
Ollesch Julian,
Schartner Jonas,
Kötting Carsten,
Genius Just,
Haußmann Ute,
Klafki Hans,
Wiltfang Jens,
Gerwert Klaus
Publication year - 2016
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.201400145
Subject(s) - peptide , protein secondary structure , attenuated total reflection , fourier transform infrared spectroscopy , chemistry , cerebrospinal fluid , infrared spectroscopy , alzheimer's disease , biophysics , chromatography , biochemistry , medicine , pathology , biology , disease , chemical engineering , organic chemistry , engineering
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.