Streptavidin binding as a model to characterize thiol-ene chemistry-based polyamine surfaces for reversible photonic protein biosensingElectronic supplementary information (ESI) available. See DOI: 10.1039/c3cc48640k

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. Polyamine-based biotin- and iminobiotin-bonded surfaces were characterized for their streptavidin-binding capacity and its reversibility in photonic biosensing with Mach-Zehnder-interferometric sensors.