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Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Article DOI: 10.3791/3560-v 08:52 min December 2nd, 2011
December 2nd, 2011



A method of using solid-state nanopores to monitor the non-specific adsorption of proteins onto an inorganic surface is described. The method employs the resistive-pulse principle, allowing for the adsorption to be probed in real-time and at the single-molecule level. Because the process of single protein adsorption is far from equilibrium, we propose the employment of parallel arrays of synthetic nanopores, enabling for the quantitative determination of the apparent first-order reaction rate constant of protein adsorption as well as and the Langmuir adsorption constant.


Solid-state Nanopores Protein Adsorption Single-molecule Measurements Nucleic Acids Protein Unfolding Binding Affinity Resistive-pulse Technique Labeling-free Measurements Transmembrane Potential Analyte Partitioning Nanopore Walls Microfluidic Devices Protein Binding Assay Nitride Films Thin Films Functionalized Surfaces Denaturing Conditions
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