Novel selective protein purification via tangential flow filtration
Dr. Andre Palmer’s lab at The Ohio State University has developed a novel purification method to isolate any target protein from a complex mixture. The process purifies a target protein (TP) from a mixture by exploiting molecular size changes that result from the formation of a protein complex consisting of a TP and its TP binding molecule (TPBM). This is accomplished via Tangential Flow Filtration (TFF). This process allows for simple and scalable purification of any protein, providing a wide range of applicability.
Proteins can be used in various medical and research applications including drug delivery, hemolysis therapies, and cancer therapies. However, purification of proteins from complex mixtures can require extensive process development. Current methods for protein purification rely on column chromatography, a costly and cumbersome process. An effective, inexpensive, and scalable method of protein purification would thus provide researchers in these areas with the capabilities that are needed for future advances in these important fields.
The technology simplifies the process of protein purification into a simple and selective system. The method exploits molecular size changes in order to isolate desired proteins via TFF. Essentially, a TPBM is used to selectively alter the size of a TP and that change in size enables the purification of the TP-TPBM complex. Upon purification of the TP-TPBM complex, the TP is dissociated and isolated.
This method represents an advancement in the field of protein purification. Current methods rely on expensive and cumbersome techniques such as column chromatography. On the other hand, this method is simple and inexpensive, enabling the advancement in several fields of science and medicine which rely on purified proteins.
A provisional patent application titled “Modeling Conditions for Tangential Flow Filtration Processes for Protein Purification" was recently filed.