MSE Seminar Series: Joseph W. Robertson, NIST

Friday, November 16, 2018
1:00 p.m.
2108 Chem/Nuc (bldg #90)
Ichiro Takeuchi

Speaker: Joseph W. Robertson, Physical Scientist @ NIST

Title: Critical interfaces for the development of electrochemical biosensors


Interfaces are at the heart of every biosensor.  Whether the sensor depends on specific biorecognition elements, low-specificity chemical interactions, or the fabrication of structured surfaces, the interface is central to a successful measurement.  The integration of complex biological molecules such as proteins with metal and semiconductor interfaces is limited by several inherent incompatibilities. To develop sensors based upon protein-protein interactions at such surfaces, three significant obstacles must be overcome: 1) the sensing protein must retain its native, or native-like structure, 2) the protein must be in electrical (or optical) contact with the metal surface and 3) the reporter protein much be at a sufficiently high concentration to produce a measurable, unambiguous signal.  In this presentation, I will discuss the fabrication of polymer-tethered bilayer membranes, which provides a biomimetic interface capable of addressing each of the three obstacles.  With inspiration taken from single molecule nanopore sensors, I will discuss the fabrication and characterization of an anthrax biosensor and discuss strategies for the  optimization and application these sensors.  


Dr. Robertson is a scientist in the Physical Measurement Laboratory at the National Institute of Standards and Technology (NIST). He received his Ph.D. in Chemistry from the University of Arizona in 2004 working under the guidance of Jeanne Pemberton. He then moved to the Max Planck Institute for Polymer Research in Mainz, Germany, where he studied biological charge transport through model lipid bilayer systems. Robertson's current research interests include advancing measurement science through biomimetic surface development, single-molecule biosensing, and new methodologies for membrane protein structure and function. 

Audience: Campus 

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