DARPA Research Associate: Department of Chemical Engineering: Troy, NY: Conducted research into the development of Protease-Containing Silicates, incorporating photo-definable UV polymerizing vinyl monomers for use as Active Antifouling Materials. These polymeric materials are the building blocks for biocatalytic coating, used in lab-on-a-chip manufacturing.
Abstract: Biocatalytic silicates, composite materials composed of alpha-chymotrypsin and a silicate prepolymer, were prepared via a two-step polymerization process, following solubilization of the enzyme in the polymerization media. This new approach resulted in active and stable composites, and a calculated half-life of over 350 days in aqueous buffer at 30 °C. The high stability and activity of this biocatalytic silicate was likely due to the covalent attachment between alpha-chymotrypsin and the silicate matrix. The protease-containing silicate was resistant to fouling by nonselective protein binding, as demonstrated by the dramatically reduced binding of human serum albumin to the silicate material when compared to that of a silicate containing pre-inactivated alpha-chymotrypsin.
NSF Scholar Research Associate: Albany Medical College, Albany, NY: Conducted research in the Department of Molecular Medicine, which revealed two major classes of fadD mutants with depressed enzyme activity.
Abstract: Fatty acyl-CoA synthetase (FACS, fatty acid:CoA ligase, AMP forming; EC 22.214.171.124) plays a central role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA. In Escherichia coli this enzyme, encoded by the fadD gene, is required for the coupled import and activation of exogenous long-chain fatty acids. The E. coli FACS (FadD) contains two sequence elements, which comprise the ATP/AMP signature motif (213YTGGTTGVAKGA224 and 356GYGLTE361) placing it in the superfamily of adenylate-forming enzymes. A series of site-directed mutations were generated in the fadD gene, within the ATP/AMP signature motif site, to evaluate the role of this conserved region to enzyme function and to fatty acid transport. My research revealed two major classes of fadD mutants with depressed enzyme activity.
NSF Scholar Research Associate: Albany Medical College, Albany, NY: Conducted research in the Department of Molecular Medicine, identifying the gene responsible for enabling Salmonella enterica serovar Typhimurium to survive carbon-starvation.
Abstract: S. typhimurium is an enteric pathogen that causes significant morbidity in humans and other mammals. During their life cycle, salmonellae must survive frequent exposures to a variety of environmental stresses, e.g. carbon-source (C) starvation. The starvation-stress response (SSR) of S. typhimurium encompasses the genetic and physiological realignments that occur when an essential nutrient becomes limiting for bacterial growth. The function of the SSR is to produce a cell capable of surviving long-term starvation. My research reported that three C-starvation-inducible lac fusions from an S. typhimurium C-starvation-inducible lac fusion library are all within a gene identified as fadF, which encodes an acyl-CoA dehydrogenase (ACDH) specific for medium-/long-chain fatty acids.