Streptavidin binding as a model to characterize thiol-ene chemistry-based polyamine surfaces for reversible photonic protein biosensing

Biotin- and iminobiotin-bonded surfaces obtained by thiol-ene chemistry and subsequent modification with polyamines were characterized with respect to streptavidin-binding capacity and reversibility for photonic biosensing using X-ray photoelectron spectroscopy and Mach-Zehnder-interferometric senso...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2014-03, Vol.50 (19), p.2424-2427
Hauptverfasser: Melnik, Eva, Muellner, Paul, Bethge, Ole, Bertagnolli, Emmerich, Hainberger, Rainer, Laemmerhofer, Michael
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container_end_page 2427
container_issue 19
container_start_page 2424
container_title Chemical communications (Cambridge, England)
container_volume 50
creator Melnik, Eva
Muellner, Paul
Bethge, Ole
Bertagnolli, Emmerich
Hainberger, Rainer
Laemmerhofer, Michael
description Biotin- and iminobiotin-bonded surfaces obtained by thiol-ene chemistry and subsequent modification with polyamines were characterized with respect to streptavidin-binding capacity and reversibility for photonic biosensing using X-ray photoelectron spectroscopy and Mach-Zehnder-interferometric sensors. The streptavidin-iminobiotin system was exploited for reversible multilayer deposition and determination of affinity constants on each layer.
doi_str_mv 10.1039/c3cc48640k
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source MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
subjects Biosensing Techniques
Biotin - analogs & derivatives
Biotin - chemistry
Dendrimers - chemistry
Photoelectron Spectroscopy
Photons
Polyamines - chemistry
Polyethyleneimine - chemistry
Protein Binding
Streptavidin - chemistry
title Streptavidin binding as a model to characterize thiol-ene chemistry-based polyamine surfaces for reversible photonic protein biosensing
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