Premium
Characterizing Binding Interactions and Elucidating 3D Structure of Aptamer‐Based Biosensors
Author(s) -
Armstrong Lindsay,
Bonham Andrew J
Publication year - 2019
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.2019.33.1_supplement.775.2
Subject(s) - aptamer , biosensor , footprinting , dna , computational biology , biophysics , dna footprinting , chemistry , conformational change , small molecule , binding site , nanotechnology , dna binding protein , biochemistry , biology , microbiology and biotechnology , transcription factor , base sequence , materials science , gene
Electrochemical DNA biosensors, whose signaling is based on signal change induced by the conformational dynamics of DNA aptamers upon target binding, have found success as sensitive and rapid methods to detect a wide variety of proteins, toxins, antibodies, and heavy metals. However, the precise mechanisms 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. Here, we have used gel mobility shift assays and dimethyl sulfate footprinting fragment analysis to investigate 3D structural interactions of DNA aptamer biosensors in the presence and absence of binding targets. These have allowed us to better characterize the individual basepair interactions involved in binding targets, as well as offer clues to the dynamic three‐dimensional folded structures of these biosensors. These results will help inform the field of biosensors and aptamers 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 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .