NDLI: Immuno-surface fabrication for biosensor optimization

Content Provider	IEEE Xplore Digital Library
Author	Danczyk, R.C. Baker, A.R. Gaba, A. Ladisch, M.R. Webster, T.J. Rundell, A.E.
Copyright Year	2002
Description	Author affiliation: Purdue Univ., West Lafayette, IN, USA (Danczyk, R.C.; Baker, A.R.; Gaba, A.; Ladisch, M.R.; Webster, T.J.; Rundell, A.E.)
Abstract	Experimental exploration and model development is being pursued for analytical determination of the best configuration and composition of immuno-surfaces for capturing target antigen. This study begins to investigate the influence of immuno-surface characteristics. Various surface chemistry fabrication techniques are compared for control of uniform-oriented antibody attachment to glass surfaces. Random orientation and non-specific attachment of antibody to the glass surface must be prevented to minimize surface heterogeneity and to maximize light-chain availability. Protein A is a binding protein that associates readily with IgG2a type antibody at the F/sub c/ region. Protein A is often used to attach antibodies and results in a surface-bound antibody that is oriented and functional with light chains free to bind antigen. This work has compared two surface chemistries, an aminosilane chemistry and a common heterobifunctional cross-linker (GMBS) technique, to evaluate their ability to covalently bind Protein A. In addition, various techniques for removing non-covalently bound protein from the glass surface were investigated and compared for effectiveness. In this manner, the present study demonstrated that GMBS covalently bound Protein A at higher densities than the aminophase technique.
Starting Page	1714
Ending Page	1715
File Size	181765
Page Count	2
File Format	PDF
ISBN	0780376129
ISSN	1094687X
DOI	10.1109/IEMBS.2002.1106616
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2002-10-23
Publisher Place	USA
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subject Keyword	Immune system Fabrication Biosensors Proteins Glass Surface treatment Chemistry Sensor phenomena and characterization Chemical technology Sensor systems
Content Type	Text
Resource Type	Article

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