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Masson JF, Battaglia TM, Davidson MJ, et al. Biocompatible polymers for antibody support on gold surfaces. Talanta. 2005;67(5):918-25doi: 10.1016/j.talanta.2005.04.023.
Masson, J. F., Battaglia, T. M., Davidson, M. J., Kim, Y. C., Prakash, A. M., Beaudoin, S., & Booksh, K. S. (2005). Biocompatible polymers for antibody support on gold surfaces. Talanta, 67(5), 918-25. https://doi.org/10.1016/j.talanta.2005.04.023
Masson, Jean-Francois, et al. "Biocompatible polymers for antibody support on gold surfaces." Talanta vol. 67,5 (2005): 918-25. doi: https://doi.org/10.1016/j.talanta.2005.04.023
Masson JF, Battaglia TM, Davidson MJ, Kim YC, Prakash AM, Beaudoin S, Booksh KS. Biocompatible polymers for antibody support on gold surfaces. Talanta. 2005 Oct 31;67(5):918-25. doi: 10.1016/j.talanta.2005.04.023. PMID: 18970259.
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Talanta. 2005 Oct 31;67(5):918-25. doi: 10.1016/j.talanta.2005.04.023.

Biocompatible polymers for antibody support on gold surfaces.

Talanta

Jean-Francois Masson, Tina M Battaglia, Michael J Davidson, Yoon-Chang Kim, Anna M C Prakash, Stephen Beaudoin, Karl S Booksh

Affiliations

  1. Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA.

PMID: 18970259 DOI: 10.1016/j.talanta.2005.04.023

Abstract

The elimination or minimization of non-specific protein adsorption from serum is critical for the use of surface plasmon resonance (SPR) sensors for in vitro and in vivo analysis of complex biological solutions. The ultimate goals in this application are to minimize non-specific adsorption of protein and to maximize analyte signal. A reduction of the non-specific protein adsorption from serum of up to 73% compared to carboxymethylated-dextran 500kDa (CM-dextran) was achieved following a survey of eight biocompatible polymers and 10 molecular weights of CM-dextran. These coatings minimize non-specific adsorption on the sensor while also serving as immobilization matrices for antibody fixation to the probes. Polymers including polysaccharides: CM-dextrans, CM-hyaluronic acid, hyaluronic acid, and alginic acid were investigated. Humic acid, polylactic acid, polyacrylic acid, orthopyridyldisuldfide-polyethyleneglycol-N-hydroxysuccinimide (OPSS-PEG-NHS), and a synthesized polymer; polymethacrylic-acid-co-vinyl-acetate (PMAVA) were also used. The non-specific protein adsorption reduction was measured over a 14 day period at 0 degrees C for each polymer. Calibration curves using some of these polymers were constructed to show the performance and low detection limit possibilities of these new antibody supports. For many of the polymers, this is the first demonstration of employment as an antibody support for an optical or surface active sensor. CM-dextran is the polymer offering the largest signal for the antigen detection. However, the biocompatible polymers demonstrate a greater stability to non-specific binding in serum. These biocompatible polymers offer different alternatives for CM-dextran.

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