About



Potomac Affinity Proteins was founded in March, 2005 to develop and commercialize technology resulting from 15 years of NIH funded research done by Dr. Philip Bryan at the University of Maryland (RO1GM42560: Folding and stability of subtilisin).   Potomac acquired the exclusive license to this technology from the University of Maryland in May, 2005.  

Potomac has been awarded three NIH SBIR awards (Small Business Innovative Research) and one USAMRIID award (United States Army Medical Research Institute for Infectious Diseases).

Grants Awarded to Potomac Affinity Proteins

1R43GM076786-01, 2R44GM076786-02  Proteases and tags for protein purification and analysis

5R43CA163403-02, 2R44CA163403-03  Protease chain reactions for molecular analysis of cancer markers

5R44GM103389-04, 5R44GM103389-05  Engineered proteases for proteomics

Details on these grants may be found at:    http://www.sbir.gov/sbirsearch/detail/278818

DOD/Defense Threat Reduction Agency  BRCALL08-Per3-2-0041   Engineering Environmentally-Stable Proteases to Specifically Neutralize Protein Toxins


Staff

Philip N. Bryan, Ph.D., Founder

Dr. Bryan has been a professor at the University of Maryland for 23 years and is a tenured professor in the Department of Bioengineering.  In his academic research, Dr. Bryan applies genetic, biochemical and biophysical methods to study protein folding and enzymology (see www.bioe.umd.edu/faculty/bryan).  

Biao Ruan, Ph.D., Chief Scientist

Before becoming Principal Scientist for Potomac Affinity Proteins in 2005, Dr. Biao Ruan worked with Dr. Bryan for 10 years on subtilisin and its interaction with the prodomain. During this time Dr. Ruan made a number of the seminal discoveries which led to the company’s first commercial products (the eXact purification system, marketed by Bio-Rad Laboratories). Dr. Ruan is considered an expert in enzymology and phage selection technology and is a co-inventor of the detection methodology.

EunJung Choi, Ph.D.

Dr. EunJung Choi has had extensive experience in both computation and experimentation in the laboratories of Dr. Brian Kuhlman at the University of North Carolina, Chapel Hill and in Ph.D. work with Stephen Mayo at the California Institute of Technology.  Her previous work has focused on the design of novel protein-protein interactions, utilizing sequence alignment information to find a scaffold protein for the interaction, then using ROSETTA and various directed evolution techniques to engineer higher affinities to the interaction.

Lauren Porter, Ph.D.

Dr. Lauren Porter has a strong background in computational design and analysis from her Ph.D. work with George Rose at the Johns Hopkins University. In this work she used general physical-chemical principles to identify and simulate short (2-4 residues) structural motifs common to the “coil” regions of high-resolution globular protein crystal structures. This work provides a physical basis for fragment assembly, currently the most successful method for protein structure prediction.



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