Reduction of nonspecific protein binding on surface plasmon resonance biosensors |
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Authors: | Jean-Francois Masson Tina M Battaglia Jeff Cramer Stephen Beaudoin Michael Sierks Karl S Booksh |
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Institution: | (1) Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA;(2) School of Chemical Engineering, Purdue University, West Lafayette, IN 47907, USA;(3) Department of Chemical and Materials Engineering, Arizona State University, Tempe, AZ 85287-6006, USA |
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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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Keywords: | Short-chain thiol CM dextran Serum adsorption Gold surfaces Biomarker detection 11-Mercaptoundecanoic acid 16-Mercaptohexadecanoic acid |
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