Issue 19, 2014

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

Abstract

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
12 Nov 2013
Accepted
25 Dec 2013
First published
09 Jan 2014
This article is Open Access
Creative Commons BY license

Chem. Commun., 2014,50, 2424-2427

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

E. Melnik, P. Muellner, O. Bethge, E. Bertagnolli, R. Hainberger and M. Laemmerhofer, Chem. Commun., 2014, 50, 2424 DOI: 10.1039/C3CC48640K

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