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 sensors. The streptavidin-iminobiotin system was exploited for reversible multilayer deposition and determination of affinity constants on each layer.
AIT Austrian Institute of Technology GmbH, Health & Environment Department, Molecular Diagnostics, 1220 Vienna, Austria. Eva.Melnik@ait.ac.at.
Eva
E
Melnik
Paul
P
Muellner
Ole
O
Bethge
Emmerich
E
Bertagnolli
Rainer
R
Hainberger
Michael
M
Laemmerhofer
D015374:Biosensing Techniques; D001710:Biotin / Q000031:analogs & derivatives* / Q000737:chemistry; D050091:Dendrimers / Q000737:chemistry*; D056951:Photoelectron Spectroscopy; D017785:Photons; D011073:Polyamines / Q000737:chemistry; D011094:Polyethyleneimine / Q000737:chemistry*; D011485:Protein Binding; D019809:Streptavidin / Q000737:chemistry*
D050091:Dendrimers; C104700:PAMAM Starburst; D011073:Polyamines; C518163:iminobiotin; D001710:Biotin; D011094:Polyethyleneimine; D019809:Streptavidin