Barney Bishop, Ph.D., Associate Professor


Dr. Bishop received a Ph.D. in chemistry from the University of North Carolina at Chapel Hill in 1997, where his graduate research focused on peptide synthesis and engineering. After receiving his doctorate, Dr. Bishop joined the laboratory of Dr. Lynne Regan at Yale University as a postdoctoral associate in order to continue his education and gain experience in the areas of molecular biology, protein engineering and protein biophysical characterization. His research focused on reengineering helical bundle proteins in order to enhance their stability. In the spring of 2001, Dr Bishop joined New River Pharmaceuticals, an early-phase pharmaceutical company focused on drug delivery, as a Senior Research Scientist. During his time at New River Pharmaceuticals, Dr. Bishop played a major role in the development of prodrug candidates for therapeutic development. He joined the Department of Chemistry and Biochemistry at George Mason University in the fall of 2003. His current research interests include molecular design, antimicrobial peptides, nanotechnolgoy and engineering hydrogel particles for biomolecular harvesting applications.

In addition to his academic efforts, Dr. Bishop sits on the scientific advisory boards for Kempharm, Inc., a biopharmaceutical company focused on the development of new and safer treatments for AD/HD and other illnesses, and Ceres Nanosciences, an early-stage biotechnology company that is commercializing biomarker-harvesting hydrogel particle technologies developed by Dr. Bishop and his collaborators in the Center for Applied Proteomics and Molecular Medicine.

Research Interests:

Cationic Antimicrobial Peptides:

Cationic antimicrobial peptides (CAMPs) are essential elements of innate immunity in higher organisms and represent a time-tested natural model for defending against bacterial and viral infections, one against which bacteria have failed to develop widespread resistance. These peptides provide a rich source of templates and strategies for the design of versatile antimicrobials to address the growing problem of antibacterial resistance and potential biothreat agents. While CAMPs appear to play a complex role in the immune response to bacterial infection, they notably exert a direct bactericidal effect. The mechanism by which these peptide kill bacteria remains poorly understood. Our research is focused on studying the physico-chemical properties of CAMPs and their role I determining selectivity and potency in order to gain insights into the mechanisms employed by these peptides and to Identify parameters that can be used to engineer CAMPs with enhanced properties. The ultimate goal being to engineer novel CAMP-based therapeutics to treat bacterial infections.

Selected Publications:

Dean, S., Bishop, B. and van Hoek, M. “Natural and synthetic cathelicidin peptides with anti-microbial and anti-biofilm activity against Staphylococcus aureus” (2011) BMC Microbiol. 11: [Epub]
De Latour, F., Amer, L., Papanastasiou, E., Bishop, B. and van Hoek, M. “Antimicrobial Activity of the Naja atra Cathelicidin and Related Small Peptides” (2010) Biochem. Biophys. Res. Comm. 396: 825-830.
Amer, L., Bishop, B. and van Hoek, M. “Antimicrobial and Antibiofilm Activity of Cathelicidins and Short, Synthetic Peptides Against Francisella” (2010) Biochem. Biophys. Res.
Papanastasiou, E. A., Hua, Q., Sandouk, A., Son, U., Christenson, A. J., van Hoek, M. L. and Bishop, B.M. “Acetylation, Charge and Antimicrobial Potency in Small Cationic Peptides Based on Human Beta-defensin-3” (2009) APMIS 117: 492-499.

Hydrogel Particle Technologies:

Functionalized hydrogel particles provide powerful tools for the isolation and concentration of low molecular weight peptides and proteins present in low abundance in complex solutions, such as serum. Hydrogel particles with incorporated affinity baits have clearly demonstrated the ability to rapidly sequester, concentrate and protect from proteolytic degradation low molecular weight proteins and peptides from serum, thereby allowing the analysis of low abundance labile biomarkers. In these particles, the highly solvated cross-linked polymer chains that comprise them provide a highly flexible and porous framework, which allows small biomolecules access to the interior space of the particle and the affinity baits that reside therein.
While our initial work focused on engineering particles for biomarker harvesting, we have expanded the scope of these studies to develop hydrogel particles for a broader spectrum of harvesting applications, including peptides, small molecule metabolites and water contaminants. Our research efforts are directed at studying how the particle framework itself and the nature of the integrated affinity baits impact the physical properties, harvesting efficiency and selectivity of the particles. This information will allow us to tailor the harvesting and physical properties of future hydrogel particles to specific applications.

Selected Publications

Patanarut, A., Williams, E., Petricoin, E., Liotta, L. and Bishop, B. “Microspheres containing Cibacron Blue F3G-A and incorporated iron oxide nanoparticles as biomarker harvesting platforms” Polymers (2011) 3: 1181-1198.
Patanarut, A., Luchini, A., Botterell, P., Mohan, A., Longo, C., Vorster, P., Petricoin, E., Liotta, L. and Bishop, B. “Synthesis and Characterization of Hydrogel Particles Containing Cibacron Blue F3G-A” Colloids and Surfaces A: Physiochem. Eng. Aspects. (2010) 362: 8-19.
Longo, C., Patanarut, A., George, T., Bishop, B., Zhou, W., Fredolini, C., Ross, M., Espina, V., Pellacani, G., Petricoin, E.F. 3rd, Liotta, L. and Luchini, A. “Core-shell Hydrogel Particles Harvest, Concentrate, and Preserve Labile Low Abundance Biomarkers” (2009) PLoS ONE 4: e4763, epub March 10
Luchini, A., Geho D.H., Bishop, B., Tran, D., Xia, C., Dufour, R.L. Jones, C. D., Espina, V., Patanarut, A., Zhou, W., Ross, M.M., Tessitore, A., Petricoin, E.F. and Liotta, L.A. “Smart Hydrogel Particles: Biomarker Harvesting: One-step Affinity Purification, Size Exclusion and Protection Against Degradation” (2008) Nano Lett. 8: 350-361.