Three-in-One Chromatography-Free Purification, Tag Removal, and Site-Specific Modification of Recombinant Fusion Proteins Using Sortase A and Elastin-like Polypeptides Academic Article uri icon

abstract

  • Column chromatography is the workhorse of protein purification, but the requirements for large volumes of buffers, expensive resins that have limited potential for re-use, and significant operator hours to optimize and execute the separations present major financial and technical hurdles to scaling up production. Additionally, covalent modification of proteins with small molecules and polymers is routine, but available conjugation methods frequently produce heterogeneous products as a result of incomplete reactivity or the presence of multiple reaction sites within a protein. These two unit operations currently present major limitations to the production of recombinant proteins at the scales necessary for both research and manufacturing. A simple process that would facilitate efficient purification as well as site-specific, covalent conjugation of small molecules to a target …

publication date

  • March 25, 2013