Researchers from Pohang University of Science and Technology have developed a new technique for purifying antiviral and anti-cancer protein therapeutics. Led by Professor Kimoon Kim, the team used the affinity interaction of cucurbiturils to purify recombinant therapeutic proteins. The technique was published recently in Nature Biomedical Engineering.
Until now, therapeutic protein purification technology has used protein-based affinity columns. However, they face financial and technological difficulties as the materials are costly, their storage or reuse is not efficient, and their suitability and efficiency depends on the properties of each therapeutic protein.
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The Postech team succeeded in purifying various types of therapeutic proteins expressed in cells by harnessing the molecular affinity interaction using a synthetic host molecule cucurbit[7]uril (or CB[7]), which they previously discovered. The molecular affinity principle, a key element in the development of the purification technique, is dependent on the high-affinity and controllable host-guest interaction between CB[7] and guests such as adamantane.
The new purification technology has succeeded in purifying a monoclonal antibody drug, Herceptin, as well as much smaller Interferon alpha (leukemia treatment) with high efficiency and high purity.
In particular, by applying small and stable synthetic molecules, the team succeeded in securing the manufacturability, sterilization, and recyclability of purified materials in a stable manner as well as increasing the purity and productivity of purified protein therapeutics. In addition, introducing adamantine (or AdA) to therapeutic proteins through genetic regulation and enzyme treatment can purify them regardless of their size or type.
This technique can be applied to most recombinant therapeutic proteins, including antibodies or fusion proteins that effectively prevent or treat fatal diseases such as viral infections or cancer, and is highly efficient and reusable, according to the team.