Eric Pang


Quantifying the Energy Within Protein-Surface Interactions

Imagine a world where pathogenic diseases can be detected accurately and rapidly to ensure instant medical diagnosis and treatment to patients, which drastically improves their chances of recovery. Most electrochemical biosensors designed to date employ synthetic DNA molecules that undergo a change in conformation upon binding of the analyte, thereby generating a signal change. However, these synthetic DNA molecules oftentimes do not come close to the chemical specificity and sensitivity of natural proteins. Protein-based biosensors therefore have the potential to significantly improve sensor performance compared to that of the current DNA-based sensor designs. So far, however, attempts at incorporating proteins into biosensors have only seen limited success and our current ability to rationally design protein-based biosensors is very limited. This limited success is a consequence of a lack of quantitative experimental techniques for measuring the effects artificial surfaces have on protein structure and function. Thus motivated, my project aims to use a new electrochemical approach to systematically measure how proximity to the polar surface used in most of the electrochemical biosensors developed by the host lab affects protein structure and function. For the first model protein we have studied, we find that the surface slightly destabilizes the folded protein. Next, we plan to study how protein function is affected by confining an enzyme to this surface. Finally, we will also explore how altering the surface chemistry affects the stability and activity of these two proteins.

UC Santa Barbara Center for Science and Engineering Partnerships UCSB California NanoSystems Institute UC Santa Barbara’s Parents Fund Campaign for UC Santa Barbara