Protein capture and identification at G-quadruplex DNA affinity surfaces

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Authors
Zhang, Tian
Issue Date
2013-12
Type
Electronic thesis
Thesis
Language
ENG
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Chemistry
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Abstract
The second part of this dissertation focuses on the fundamental characterization of affinity surfaces. Specifically, we studied affinity protein capture at G-quadruplex-forming-aptamer-modified surfaces using imaging tools. Two systems were used to investigate the DNA-modification and protein capture characteristics of different affinity surfaces: first, thrombin binding aptamer (TBA) and a control oligo sequence with no G-quadruplex forming ability, and second, the Pu28-mer sequence. The affinity surfaces of interest included fused silica plates, streptavidinated magnetic beads, and indium tin oxide (ITO)-coated glass slides. The results of these experiments provide a better fundamental understanding of protein capture at aptamer-modified surfaces that might lead to improved design and reliability of devices and processes for protein analysis, separation, isolation and purification.
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December 2013
School of Science
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Rensselaer Polytechnic Institute, Troy, NY
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