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The action/adventure game Grad School: HGH is the final, extended version of a BME Prototyping class project in which the goal was to produce a zombie-themed game that teaches biomedical engineering concepts. The gameplay provides fast paced, exciting, and mildly addicting rooms that the player must battle and survive through,

The action/adventure game Grad School: HGH is the final, extended version of a BME Prototyping class project in which the goal was to produce a zombie-themed game that teaches biomedical engineering concepts. The gameplay provides fast paced, exciting, and mildly addicting rooms that the player must battle and survive through, followed by an engineering puzzle that must be solved in order to advance to the next room. The objective of this project was to introduce the core concepts of BME to prospective students, rather than attempt to teach an entire BME curriculum. Based on user testing at various phases in the project, we concluded that the gameplay was engaging enough to keep most users' interest through the educational puzzles, and the potential for expanding this project to reach an even greater audience is vast.
ContributorsNitescu, George (Co-author) / Medawar, Alexandre (Co-author) / Spano, Mark (Thesis director) / LaBelle, Jeffrey (Committee member) / Guiang, Kristoffer (Committee member) / Barrett, The Honors College (Contributor) / Harrington Bioengineering Program (Contributor)
Created2014-05
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Description
Research concerning increased sensitivity and accurate glucose sensors have been on the forefront of diabetes mellitus. In this study, Electroactive Poly-Amidoamine Polymer (EPOP) was studied to determine if it can be used as a biocompatible electrode, with known redox mediators to determine if it can transfer its own electrons or

Research concerning increased sensitivity and accurate glucose sensors have been on the forefront of diabetes mellitus. In this study, Electroactive Poly-Amidoamine Polymer (EPOP) was studied to determine if it can be used as a biocompatible electrode, with known redox mediators to determine if it can transfer its own electrons or amplify signal, and if signal is amplified when using an Ag/AgCl working electrode. From the results, it was determined that EPOP is neither a redox mediator, since it cannot transfer its own electrons, nor an electron mediator, since it does not amplify measured current at a specific voltage. Rather, it behaves as an electron sink capacitor with inconsistent behavior when Ag/AgCl is used as the working electrode with the redox mediator alone or with the redox mediator using in combination with glucose oxidase (GOx) and glucose. This was validated using AC-Impedance which gave a -3.3999 slope for isolated 0.05 g/mL EPOP in solution and R2 value of 0.992 displaying it had more capacitor-like behavior compared to resistor-like behavior. For this reason, EPOP was infused into a carbon screen-printed electrode by adding it dissolved and undissolved at two levels into carbon ink. The effectiveness of this electrode was tested using a potentiostatic CV. For the 0.1 g/mL EPOP dissolved in carbon ink, the reduction voltage peak (0.18 V) was found to be slightly higher than a GDE (0.14 V); however, the measured current was found to be 1.57 times the amplitude of a GDE. When 0.05 g/mL EPOP in PBS dissolved in graphite ink was used to detect glucose as the working electrode, there was increased signal amplification, and therefore, increased sensitivity to glucose when using EPOP infused electrodes. This offers promising results for disposable glucose sensors.
ContributorsKapadia, Meera Vipul (Author) / LaBelle, Jeffrey (Thesis director) / Islam, Rafiqul (Committee member) / Honikel, Mackenzie (Committee member) / Chemical Engineering Program (Contributor) / Barrett, The Honors College (Contributor)
Created2017-05
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Description
A point of care glucose sensor using electrochemical impedance spectroscopy (EIS) with a glutaraldehyde-linked enzyme shows promise as an effective biosensor platform. This report details the characterization of various factors on optimal binding frequency (OBF) and sensor performance to better prepare the sensor for future experimentation. Utilizing a screen printed

A point of care glucose sensor using electrochemical impedance spectroscopy (EIS) with a glutaraldehyde-linked enzyme shows promise as an effective biosensor platform. This report details the characterization of various factors on optimal binding frequency (OBF) and sensor performance to better prepare the sensor for future experimentation. Utilizing a screen printed carbon electrode, the necessary amount of glucose oxidase was determined to be 10 mg/mL. Binding time trials ranging from 1-3 minutes demonstrated that 1.5 minutes was the optimal binding time. This timeframe produced the strongest impedance response at each glucose concentration. Using this enzyme concentration and binding time, the native OBF of the biosensor was found to be 1.18 Hz using vector analysis. Temperature testing showed little change in OBF in sensors exposed to 4 \u00B0C through 43.3 \u00B0C. Only exposure to 60 \u00B0C resulted in rapid OBF change which was likely due to glucose oxidase becoming denatured. Humidity tests showed little change in OBF and sensor performance between sensors prepared at the humidities of 7.5%, 10.625% and 16.5% humidity. Alternatively, solutions containing common interference molecules such as uric acid, acetaminophen, and ascorbic acid resulted in a highly shifted OBF and drastically reduced signal.
ContributorsMatloff, Daniel (Co-author) / Khanwalker, Mukund (Co-author) / Johns, Jared (Co-author) / LaBelle, Jeffrey (Thesis director) / Pizziconi, Vincent (Committee member) / Lin, Chi (Committee member) / Dean, W.P. Carey School of Business (Contributor) / School of Life Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2018-12