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Structure and Performance of DNA Biosensors


EMSL Project ID
9605

Abstract

Biosensors typically rely on designing a surface that is functionalized with biomolecules that specifically bind analytes of interest. These surfaces often include specific oligonucleotide sequences for DNA hybridization, antibodies for binding proteins or chemicals, aptamers (3-d nucleic acid structures) for binding biomolecules, or other types of ligands. The conformation of the biomolecules on the surface is important both before and after specific binding. Before specific binding, the conformation must provide binding sites that are accessible to the analytes. After specific binding, there is often a conformational change that can be used to measure the binding interaction. In addition, the surface chemistry should be designed to minimize non-specific binding that will interfere with specific binding and detection, either by blocking accessibility of the analytes of interest, or by producing an additional signal that increases the background (and therefore negatively affects the detection limit). Understanding the factors that affect the biomolecular conformation on biosensor surfaces will aid in the rational design of the most selective, sensitive, and rapid biosensor systems.

DNA microarrays are one example of a widely used biosensor surface in which an understanding of the factors affecting selectivity, sensitivity, and response time could improve the performance of the sensors. Currently, non-specific binding to DNA microarray elements is a problem that results in an inherent background signal that decreases system sensitivity. In addition, response times for selective sensing are typically on the order of hours. The aim of this project will be to use in situ neutron scattering to investigate the conformation of DNA microarrays before and after specific hybridization, and correlate this data with the DNA microarray performance (selectivity, sensitivity and response time).

Project Details

Project type
Exploratory Research
Start Date
2004-06-25
End Date
2005-08-11
Status
Closed

Team

Principal Investigator

Cindy Bruckner-Lea
Institution
Pacific Northwest National Laboratory

Team Members

Timothy Straub
Institution
Pacific Northwest National Laboratory

Scott Lea
Institution
Environmental Molecular Sciences Laboratory

Related Publications

Kajimoto M., D.R. Ledee, A. Olson, N.G. Isern, I. Robillard Frayne, C. Des Rosiers, and M.A. Portman. 2016. "Selective cerebral perfusion prevents abnormalities in glutamate cycling and neuronal apoptosis in a model of infant deep hypothermic circulatory arrest and reperfusion." Journal of Cerebral Blood Flow and Metabolism 36, no. 11:1992-2004. PNNL-SA-118083. doi:10.1177/0271678X16666846