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UV-SPR biosensor for biomolecular interaction studies
Author(s): F. A. Geiss; S. Fossati; I. Khan; N. Gisbert Quilis ; W. Knoll; J. Dostalek
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Paper Abstract

UV surface plasmon resonance (SPR) for direct in situ detection of protein binding events is reported. A crossed relief aluminum grating was employed for diffraction coupling to surface plasmons as an alternative to more commonly used attenuated total reflection method. Wavelength interrogation of SPR was carried out by using transmission measurements in order to probe odorant-binding protein 14 (OBP14) of the honey bee (Apis mellifera). The native oxide layer on the top of an aluminum grating sensor chip allows for covalent coupling of protein molecules by using regular silane-based linkers. The probing of bound OBP14 protein at UV with confined field of surface plasmons holds potential for further studies of interaction with recently developed artificial fluorescent odorants.

Paper Details

Date Published: 16 May 2017
PDF: 8 pages
Proc. SPIE 10231, Optical Sensors 2017, 1023107 (16 May 2017); doi: 10.1117/12.2265683
Show Author Affiliations
F. A. Geiss, AIT Austrian Institute of Technology GmbH (Austria)
Univ. of Natural Resources and Life Sciences (Austria)
S. Fossati, AIT Austrian Institute of Technology GmbH (Austria)
I. Khan, AIT Austrian Institute of Technology GmbH (Austria)
N. Gisbert Quilis , AIT Austrian Institute of Technology GmbH (Austria)
W. Knoll, AIT Austrian Institute of Technology GmbH (Austria)
J. Dostalek, AIT Austrian Institute of Technology GmbH (Austria)


Published in SPIE Proceedings Vol. 10231:
Optical Sensors 2017
Francesco Baldini; Jiri Homola; Robert A. Lieberman, Editor(s)

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