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Reduction of nonspecific protein binding on surface plasmon resonance biosensors

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Abstract

Reduction of the nonspecific serum protein adsorption on a gold surface to levels low enough to allow the detection of biomarkers in complex media has been achieved using the N-hydroxysuccinimide (NHS) ester of 16-mercaptohexadecanoic acid. Carboxymethylated dextran (CM dextran), which is widely used, nonspecifically adsorbs enough proteins to mask the signal from target biomarkers in complex solutions such as serum or blood. The use of short-chain thiols greatly reduces the amount of nonspecific protein adsorption. Mixed layers of 11-mercaptoundecanoic acid or the NHS ester of 11-mercaptoundecanoic acid mixed layers with either 11-mercaptoundecanol or undecanethiol, and 16-mercaptohexadecanoic acid or the NHS ester of 16-mercaptohexadecanoic acid with hexadecanethiol, were also investigated for nonspecific protein binding properties as well as for biomarker signal response. The NHS ester of 16-mercaptohexadecanoic acid exhibits the largest signal for the biomarker myoglobin (including CM dextran) while offering a significantly diminished amount of nonspecific binding. The sensor has also been shown to detect interleukin-6 in cell culture media containing protein concentrations of at least 4 mg/mL.

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Acknowlegments

This work was sponsored by the National Institutes of Health, National Institute of Biomedical Imaging and Biosensors (NIBIB), award number R01EB004761, by the American Heart Association (AHA), award number 0151218Z, and Arizona State University. The NMR studies were conducted by Dr. Ronald Nieman of Arizona State University.

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Authors and Affiliations

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

    Jean-Francois Masson, Tina M. Battaglia, Jeff Cramer & Karl S. Booksh

  2. School of Chemical Engineering, Purdue University, West Lafayette, IN, 47907, USA

    Stephen Beaudoin

  3. Department of Chemical and Materials Engineering, Arizona State University, Tempe, AZ, 85287-6006, USA

    Michael Sierks

Authors
  1. Jean-Francois Masson
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  2. Tina M. Battaglia
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  3. Jeff Cramer
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  4. Stephen Beaudoin
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  5. Michael Sierks
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  6. Karl S. Booksh
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Corresponding author

Correspondence to Karl S. Booksh.

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Masson, JF., Battaglia, T.M., Cramer, J. et al. Reduction of nonspecific protein binding on surface plasmon resonance biosensors. Anal Bioanal Chem 386, 1951–1959 (2006). https://doi.org/10.1007/s00216-006-0834-2

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  • DOI: https://doi.org/10.1007/s00216-006-0834-2

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