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Gosselin E, Vanden Eynde JJ, Petit A, et al. Designing a high performance, stable spectroscopic biosensor for the binding of large and small molecules. J Colloid Interface Sci. 2017;508:443-454doi: 10.1016/j.jcis.2017.08.057.
Gosselin, E., Vanden Eynde, J. J., Petit, A., Conti, J., & De Coninck, J. (2017). Designing a high performance, stable spectroscopic biosensor for the binding of large and small molecules. Journal of colloid and interface science, 508443-454. https://doi.org/10.1016/j.jcis.2017.08.057
Gosselin, E, et al. "Designing a high performance, stable spectroscopic biosensor for the binding of large and small molecules." Journal of colloid and interface science vol. 508 (2017): 443-454. doi: https://doi.org/10.1016/j.jcis.2017.08.057
Gosselin E, Vanden Eynde JJ, Petit A, Conti J, De Coninck J. Designing a high performance, stable spectroscopic biosensor for the binding of large and small molecules. J Colloid Interface Sci. 2017 Dec 15;508:443-454. doi: 10.1016/j.jcis.2017.08.057. Epub 2017 Aug 24. PMID: 28858654.
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J Colloid Interface Sci. 2017 Dec 15;508:443-454. doi: 10.1016/j.jcis.2017.08.057. Epub 2017 Aug 24.

Designing a high performance, stable spectroscopic biosensor for the binding of large and small molecules.

Journal of colloid and interface science

E Gosselin, J Jacques Vanden Eynde, A Petit, J Conti, J De Coninck

Affiliations

  1. Laboratory of Physics of Surfaces and Interfaces, LPSI, University of Mons, Place du Parc 23, B-7000 Mons, Belgium. Electronic address: [email protected].
  2. Laboratory of Organic Chemistry, University of Mons, Av Maistriau, B-7000 Mons, Belgium. Electronic address: [email protected].
  3. Laboratory of Physics of Surfaces and Interfaces, LPSI, University of Mons, Place du Parc 23, B-7000 Mons, Belgium.

PMID: 28858654 DOI: 10.1016/j.jcis.2017.08.057

Abstract

In the context of FTIR ATR-based sensors, the organic layer covering the ATR element has to be as stable as possible for optimal spectroscopic measurements. Previously, this self-assembled covering was considered stable after several hours under a PBS flux, probably due to a hydrophobic barrier, which prevents water penetration into the grafted network. Stability and reactivity, measured simultaneously using FTIR ATR, identify the limits of the previously used molecular construction. For the first time, surface etching of the previous functionalised Ge devices (Ge-PEG-NHS), a few minutes after BSA injection, was observed. It was concluded that the molecular chain deformation of Ge-PEG-NHS likely occurred when large molecules were bound. BSA loaded onto a Ge-PEG-NHS surface led to network deprotection, with the probable disruption of hydrogen bonds for single barrier-based networks. This, in turn, was presumably influenced by the random deposition of the NHS moiety on the PEG chain. A new functionalised germanium device, using a rapid three-step in situ procedure, provides an efficient robust network composed of two protective barriers, ideal for the binding of various sized molecules. The Ge-APS-PEG-NHS device has shown exceptional sensitivity with regards to BSA and ethanolamine target molecules while offering homogeneous NHS distribution.

Copyright © 2017 Elsevier Inc. All rights reserved.

Keywords: Biosensors; FTIR ATR spectroscopy; Germanium; Grafting; In situ functionalisation; Label free; Large molecule; Organic layer; Small molecule; Stability

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