Incorporating Functional Nanomaterials in Layer-by-Layer Amperometric Sensor Designs: Adaptable Templates for Clinically Relevant Measurements
Professor Michael Leopold | University of Richmond
Hosted by Professor Rebecca Pompano
Research and development of materials and strategies for real-time, amperometric sensors and biosensors with potential in-vitro or in-vivo applications for clinically relevant physiological agents continues to be a relevant scientific endeavor. Within this field of study, a large number of reports continue to focus on enzyme-based glucose detection because it serves both as a well-understood fundamental model system and as a clinically relevant sensing goal for diabetics. It is, however, relatively rare that the same strategies and materials utilized for glucose sensing prove to be robust and versatile enough to be readily adapted to different target molecules with clinical relevance. It follows then that a significant achievement would be the demonstration of a strategy and the use of materials that offer this type of versatility while maintaining superior performance toward a molecule with bioanalytical implications and possible medical applications. Our work explores layer-by-layer (LbL) strategies for amperometric biosensor and sensor designs, where each layer or material within the composite film, including the incorporation of different nanomaterials, is functional with respect to sensing sensitivity and/or selectivity. Additionally, this research also involves sensor development toward practical and effective clinical usage where the LbL strategies must be successfully adapted and miniaturized to needle or wire electrodes that can potentially function in vitro as a bedside device, within catheters for continuous, real-time measurements, or as an in vivo implant operating in biological media and physiologically relevant concentrations. Fundamental studies proceed with a glucose model system before adapting the strategy and materials to specifically targeted clinical measurements including early detection/monitoring for sepsis, pregnancy-induced hypertension, and prostate cancer among others.
Spontaneous Formation of Oligomers and Fibrils in Large Scale Molecular Dynamics Simulations of the Alzheimer’s Peptides
Professor Carol Hall | North Carolina State University
Hosted by Professor Kateri DuBay
Spontaneous Formation of Oligomers and Fibrils in Large-Scale Molecular Dynamics Simulations of the Alzheimer’s Peptides
Protein aggregation is associated with serious and eventually-fatal neurodegenerative diseases including Alzheimer’s, Parkinson’s and the prion diseases. While atomic resolution molecular dynamics simulations have been useful in this regard, they are limited to an examination of either oligomer formation by a small number of peptides or analysis of the stability of a moderate number of peptides placed in trial or known experimental structures. We describe large-scale molecular dynamics simulations of the spontaneous formation of fibrils by systems containing large numbers of peptides. The simulations are fast enough to enable us to follow the steps in the aggregation process from an initial configuration of random coils to oligomers and then to proto-filaments with cross-β structures. In simulations of Aβ17-42 peptides, we uncovered two fibrillization mechanisms that govern their structural conversion from disordered oligomers into protofilaments. We also investigate the influence of crowding agents on oligomerization and fibrillization for Aβ16-22. Simulations are conducted which allow examination of the impact of naturally-derived inhibitors (resveratrol, curcumin, vanillin, and curcumin) on the oligomerization and fibrillation of A β17-36. Finally, we describe simulations of human, mouse and Syrian Movies of the aggregation process on a molecular level will be shown.
Jefferson Lecture (title TBA)
Professor David MacMillan | Princeton University
Hosted by Graduate Student Council
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