DEEPs - De novo Expression Enhancer Proteins for Improved Protein Expression and Purification

Web Published:

Princeton Docket # 17-3357-1


To improve the production of biomedically important peptides and proteins that are challenging to express with recombinant DNA technology, researchers at Princeton University have created a collection of synthetic genes to encode highly stable de novo proteins for use as genetic fusion tags. The resulting method has been shown to enhance expression level, improve solubility, decrease degradation, and favor folding of the proteins and peptides of interest. This new composition of genes are small (~100 amino acids) and therefore do not impose a significant burden on the cell’s protein expression machinery. This method also allows for rapid purification without addition of supplemental affinity tag for use with wide-spread purification technology such as Ni-IMAC. Several proteins of interest have been demonstrated to be produced in superior quantities using this novel method compared to those fused to SUMO, a commercially available well-known fusion tag of comparable size.



•       Production of difficult sequences: poor expression, prone to degradation, toxic or unstructured.

•       Isotopically labeled proteins, proteins of different hosts, pull down assays, surface immobilization, fluorescent labeling.

•       High throughput screening collections of mutated proteins of interest for better stability and function.



•       Improved expression, solubility, stability, and folding.

•       Small (~100 amino acids)

•       Do not require additional affinity tag for use in Ni-IMAC.

•       Simultaneous fusion of POI to both N- and C-termini.


The Inventors:


Michael Hecht is a Professor of Chemistry. Research in the Hecht group focuses in two areas: Synthetic biology and Alzheimer's disease. The group devises novel proteins by designing amino acid sequences that fold into a specific 3-dimensional structure. They also seek to understand how protein in Alzheimer disease mis-fold into oligomeric or fibrillar structures. Professor Hecht has received numerous award for his research excellence, most notably Kaiser Award (Protein Society, 2003), Beckman Young Investigator Award (1993), and Whitaker Foundation Young Investigator Award (1992).


Shlomo Zarzhitsky is a postdoctoral researcher in Prof. Hecht’s lab. Shlomo is a biotechnology engineer with extensive experience in the design and characterization of peptides. Owing to his interest in applied research, Shlomo is currently investigating the ability of designed proteins to chaperone and facilitate the production of biopharmaceuticals.


Intellectual Property Status:

Patent protection is pending.

Princeton is seeking to identify appropriate partners for the further development and commercialization of this technology.




Cortney Cavanaugh

Princeton University Office of Technology Licensing • (609) 258-7256•




Patent Information:
For Information, Contact:
Cortney Cavanaugh
New Ventures and Licensing associate
Princeton University
Michael Hecht
Shlomo Zarzhitsky