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Synthetic Biology and Interfacial Catalysis

US Naval Research Laboratory, Washington, District of Columbia

Position Description:
Postdoctoral research positions are available immediately in the Center for Bio/Molecular Science and Engineering at the US Naval Research Laboratory, Washington DC (http://www.nrl.navy.mil/). This position is at the interface of biology and materials and focuses on creating new biocataltyic enzyme-based nanomaterials with emergent properties.

The Naval Research Laboratory is the Department of Defense's corporate laboratory for the Navy and Marine Corps. The Center for Bio/Molecular Science and Engineering works at the interface of materials, chemistry, biology, biophysics and materials science to solve critical problems of importance to the Navy and DoD.

Project Description:
When enzymes are displayed at a nanoparticle interface in a controlled and homogeneous manner, in many cases they display substantially enhanced catalytic activity. We are interested in understanding the mechanisms by which enzyme activity is altered and enhanced at this nanoparticle interface and learning how to exploit this. We are particularly interested in designing and assembling totally artificial enzyme-based biosynthetic pathways on nanoparticles in vitro where the overall catalytic flux through the system can be expected to be greatly enhanced by what appears to be channeling behavior. This approach represents an important and complementary way of achieving biocatalysis for synthetic biology that is still extremely underutilized.

In many instance enzymes also have a propensity to lose activity rapidly when removed from the cellular environment. Often this phenomenon can be countered through direct engineering of the enzyme or tailoring of reaction conditions. These processes, however, are not always conducive to applications that rely on the distribution of enzymes systems into complex or uncontrolled environments. In nature, microbes frequently package cellular products into stable membrane vesicles that are released into the environment. Our research focuses on harnessing this process to facilitate the production and encapsulation of enzymes and other cellular products into bacterial membrane vesicles to facilitate processes such as bioremediation, cell delivery, and microbial community manipulation.

Qualifications:
Candidate experience and required skill set include a PhD in a related biological discipline such as molecular biology, biochemistry, or microbiology with some combination of experience in cloning and recombinant DNA technology, enzymatic assays, fluorescence, bacterial-eukaryotic cell expression and analysis, biosensing, and synthetic biology. Experience with nanoparticles/nanomaterials and FRET are a plus.
Salary: $77,490/year with health benefits plus travel allotment.

To Apply:

The position is administered through the National Research Council. FOr more information and to apply online, please visit: https://www.nrl.navy.mil/careers/post-doc/nrc/

Point of Contact:
Igor L. Medintz Ph.D (S&T)
Senior Scientist for Biosensors and Biomaterials
Center for Bio/Molecular Science and Engineering
U.S. Naval Research Laboratory Code 6907
Washington D.C., 20375 USA

Representative publications:

  • Vranish, J.N., Ancona, M.G., Oh, E., Oh, E., Susumu, K., Medintz, I.L. Enhancing Coupled Enzymatic Activity by Conjugating One Enzyme to a Nanoparticle. Nanoscale 9, 5172-5187 (2017).
  • Ding, S., Cargill, A.A., Medintz, I.L., Claussen, J.C. Increasing the Activity of Immobilized Enzymes with Nanoparticle Conjugation. Current Opinion in Biotechnology 34, 242-250 (2015).
  • Claussen, J.C., Malanoski, A., Breger, J.C., Oh, E., Walper, S.A., Susumu, K., Goswami, R., Deschamps, J.R., Medintz, I.L. Probing the Enzymatic Activity of Alkaline Phosphatase Within Quantum Dot Bioconjugates. The Journal of Physical Chemistry C 119, 2208-2221 (2015).
  • Breger, J.C., Ancona, M.G., Walper, S.A., Oh, E., Susumu, K., Stewart, M.H., Deschamps, J.R., Medintz, I.L. Understanding How Nanoparticle Attachment Enhances Phosphotriesterase Kinetic Efficiency. ACS Nano 8, 8491-8503 (2015).
  • Johnson, B.J., Algar, W.R., Malanoski, A.P., Ancona, M.G., Medintz, I.L. Understanding Enzymatic Acceleration at Nanoparticle Interfaces: Approaches and Challenges. Nano Today 9, 102-131 (2014).
  • Algar, W. R., Malonski, A., Deschamps, J.R., Blanco-Canosa, J.B., Susumu, K., Stewart, M.H., Johnson, B.J., Dawson, P.E. and Medintz, I.L. Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial "Hopping". Nano Letters 12, 3793-3802 (2012).