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The Washington Research Foundation Fellowship

Jared Houghtaling - Bioengineering: Nanoscience & Molecular Engineering

Jared Houghtaling Jared Houghtaling joined the joint lab of Professors Paul Yager, Barry Lutz, and Elain Fu during his freshman year, and working in the lab has since opened the doors to biomedical research as a career. Now a senior In the Department of Bioengineering, Jared was drawn to innovating solutions that expand access to healthcare. His desire to pursue research on porous membrane-based diagnostics is largely motivated by the fact that many people in the developing world die from curable diseases because of a lack of appropriate testing. Accurate diagnostic tools can save countless lives and improve quality of living all over the globe. Alongside his mentor, Dr. Elain Fu, he has designed and patented a novel porous membrane-based valving method to further automate and sophisticate diagnostic assays. Jared is currently working on a novel displacement based assay, designed to detect small molecules, which would be used for food/water safety, rapid detection of the stress hormone cortisol, and drugs-of-abuse testing. He plans to carry on with his passion for biomedical research by pursuing a Ph.D. in bioengineering. Outside of the lab, Jared is an active UW Biomedical Engineering Society Officer, serving as the organization’s president this year. He is also an officer on the Global Health Undergraduate Leadership Committee, and coordinates various bioengineering and global health outreach events for undergraduates and local high school students. In his fleeting spare time, he enjoys cycling, playing the guitar, and spending time with friends and family.

Mentor: Elain Fu, Bioengineering

Project Title: Development of a Displacement Format, Porous Membrane-Based Diagnostic for Small Molecule Detection

Abstract: Porous membrane-based lateral flow assays have become very popular for the diagnosis of a wide range of conditions. Attributes of these assays vary drastically depending upon application. Most commercially available lateral flow tests (LFTs) employ a ‘sandwich’ format, where the target molecule is effectively sandwiched between a surface anchored antibody and a visibly labeled antibody. Because small molecules lack multiple epitopes (antibody binding sites), they cannot support the binding of two antibodies simultaneously, and thus cannot be detected using a sandwich format. Competition format assays offer a solution to this problem, allowing target analyte in the testing sample to compete for surface-anchored antibody binding sites with pre-bound, conjugated analyte. The subsequent displacement of conjugated analyte (loss of visible signal) is then correlated with concentration of analyte in the sample. However, competition assay techniques fall short in two key areas: they rely on a counterintuitive, inverted user read-out where a darker signal translates to lower concentration, and they lack the ability to chemically amplify signals. My work seeks to modify and improve current competition methods by capturing the displaced, conjugated analyte downstream using a complimentary protein binding pair (e.g. streptavidin and biotin). Captured analyte could then be labeled using gold-nanoparticle antibody conjugates or enzymatic colorimetric chemistries to produce a very sensitive positive signal. The ultimate goal is to develop a ‘displacement format’ assay in a porous membrane network that greatly improves the limit of detection for small molecules and short peptide sequences. Specific applications include: rapid detection of cortisol to diagnose post-traumatic stress disorder or Cushing’s disease, therapeutic monitoring of HIV, TB, and epilepsy biomarkers, and field-use testing for active drug components like Δ9 THC in marijuana. Such an assay would have tremendous utility at the point-of-care, and would provide an efficient and effective alternative to expensive lab-based testing.