Enhanced biosensor performance using an avidin-biotin bridge for antibody immobilization

Upvan Narang; George P. Anderson; Keeley D. King; Heidi S. Liss; Frances S. Ligler

doi:10.1117/12.273534

7 May 1997 Enhanced biosensor performance using an avidin-biotin bridge for antibody immobilization

Upvan Narang, George P. Anderson, Keeley D. King, Heidi S. Liss, Frances S. Ligler

Proceedings Volume 2980, Advances in Fluorescence Sensing Technology III; (1997) https://doi.org/10.1117/12.273534
Event: BiOS '97, Part of Photonics West, 1997, San Jose, CA, United States

Abstract

Maintaining antibody function after immobilization is critical to the performance of a biosensor. The conventional methods to immobilize antibodies onto surfaces are via covalent attachment using a crosslinker or by adsorption. Often, these methods of immobilization result in partial denaturation of the antibody and conformational changes leading to a reduced activity of the antibody. In this paper, we report on the immobilization of antibodies onto the surface of an optical fiber through an avidin-biotin bridge for the detection of ricin, ovalbumin, and Bacillus globigii (Bg). The assays are performed in a sandwich format. First, a capture antibody is immobilized, followed by the addition of the analyte. Finally, a fluorophore- labeled antibody is added for the specific detection of the analyte. The evanescent wave-induced fluorescence is coupled back through the same fiber to be detected using a photodiode. In all cases, we observe an improved performance of the biosensor, i.e., lower limit of detection and wide linear dynamic range, for the assays in which the antibody is immobilized via avidin-biotin bridges compared to covalent attachment method.

Citation Download Citation

Upvan Narang, George P. Anderson, Keeley D. King, Heidi S. Liss, and Frances S. Ligler "Enhanced biosensor performance using an avidin-biotin bridge for antibody immobilization", Proc. SPIE 2980, Advances in Fluorescence Sensing Technology III, (7 May 1997); https://doi.org/10.1117/12.273534

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available