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Characterizing Binding Interactions and Elucidating Structure of Aptamer‐Based Biosensors
Author(s) -
Armstrong Lindsay Therese,
Bonham Andrew J.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.657.4
Subject(s) - aptamer , biosensor , förster resonance energy transfer , biophysics , nucleic acid , chemistry , dna , nanotechnology , computational biology , small molecule , biochemistry , fluorescence , biology , microbiology and biotechnology , materials science , physics , quantum mechanics
Electrochemical biosensors based on the conformational dynamics of DNA aptamers have found success against a wide variety of proteins, toxins, antibodies, and heavy metals. However, the mechanistic underpinnings of the mechanism by which these surface‐bound DNA molecules change conformation upon target binding, thus changing the dynamics of an appended redox‐active tag and generating a measurable signal, is poorly understood. Our first target for investigation was a previously reported Ricin Chain A binding aptamer biosensor. Here, we have investigated this biosensor using a variety of nucleic acid assays, including PCR‐termination via basepair modification, fluorescence anisotropy, gel mobility shift assays, and FRET tagging to determine 3D orientation. These have allowed us to better characterize the basepair interactions involved in binding targets, as well as offer clues to the changing three dimensional folded structures of these biosensors. These results will help inform the field of biosensors and aptamers in general on strategies for future optimization. Support or Funding Information This work is supported by internal grant funding from the Metropolitan State University of Denver. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .