Investigation of biotin-streptavidin binding interactions using microcantilever sensors.
We report the investigation of biotin-streptavidin binding interactions using microcantilever sensors. A symmetric cantilever construction is employed to minimize the effects of thermal drift and the control of surface chemistry on the backside of the cantilever is demonstrated to reduce the effects of non-specific binding interactions on the cantilever. Three structurally different biotin modified cantilever surfaces are used as a model system to study the binding interaction with streptavidin. The cantilever response to the binding of streptavidin on these biotin sensing monolayers is compared. The lowest detection limit of streptavidin using biotin-HPDP is found to be between 1 and 10nM limited by the optical measurement setup. Surface characterization using quartz crystal microbalance (QCM) and high-resolution atomic force microscope (AFM) is used to benchmark the cantilever sensor response. In addition, the QCM and AFM studies reveal that the surface density of bound streptavidin on biotin modified surfaces was low, thereby implying that effects other than steric hindrance are responsible for defining cantilever response.
Shu
Wenmiao
W
The Nanoscience Centre, University of Cambridge, 11 J.J. Thomson Avenue, Cambridge CB3 0FF, UK.
Laue
Ernest D
ED
Seshia
Ashwin A
AA
D000327:Adsorption; D015374:Biosensing Techniques; D001710:Biotin / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D019809:Streptavidin / Q000378:metabolism* / Q000493:pharmacokinetics
D001710:Biotin; D019809:Streptavidin