Abstract
Streptavidin was used as a linker protein for binding a second biotinylated protein. To efficiently combine streptavidin without non-specific binding, a well-controlled array of biotin was prepared on a gold surface by a mixed self-assembly method. Two thiol derivatives containing hydroxyl and biotin functional groups, respectively, were used to fabricate the mixed self-assembled monolayer. The antibody was fragmented, modified with biotin, and added to the array on the streptavidin linker layer. Topographical changes to the array surface caused by protein immobilization were demonstrated by applying atomic force microscopy and ellipsometry. The resonance wavelengths of SPR spectra were red shifted according to the increase in thickness of the dielectric layer by protein immobilization.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Colloids and Surfaces A: Physicochemical and Engineering Aspects
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.