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

Chem Commun (Camb). 2014 Mar 7;50(19):2424-7. doi: 10.1039/c3cc48640k. Epub 2014 Jan 22.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques*
  • Biotin / analogs & derivatives*
  • Biotin / chemistry
  • Dendrimers / chemistry*
  • Photoelectron Spectroscopy
  • Photons
  • Polyamines / chemistry
  • Polyethyleneimine / chemistry*
  • Protein Binding
  • Streptavidin / chemistry*

Substances

  • Dendrimers
  • PAMAM Starburst
  • Polyamines
  • iminobiotin
  • Biotin
  • Polyethyleneimine
  • Streptavidin