Purification of protein therapeutics via high-affinity supramolecular host-guest interactions
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SCOPUS
- Title
- Purification of protein therapeutics via high-affinity supramolecular host-guest interactions
- Authors
- Jaeyeon An; Sungwan Kim; Annadka Shrinidhi; Junghyun Kim; Hasanul Banna; Gihyun Sung; Kyeng Min Park; Kimoon Kim
- Date Issued
- 2020-07
- Publisher
- NATURE PUBLISHING GROUP
- Abstract
- Efficient purification is crucial to providing large quantities of recombinant therapeutic proteins, such as monoclonal antibodies and cytokines. However, affinity techniques for manufacturing protein therapeutics that use biomolecule-conjugated agarose beads that harness specific biomolecular interactions suffer from issues related to protein denaturation, contamination and the need to maintain biomolecule-specific conditions for efficient protein capture. Here, we report a versatile and scalable method for the purification of recombinant protein therapeutics. The method exploits the high-affinity and controllable host-guest interactions between cucurbit[7]uril (CB[7]) and selected guests such as adamantylammonium. We show that the Herceptin (the brand name of trastuzumab, a monoclonal antibody drug used to treat breast cancer) and the much smaller cytokine interferon alpha-2a can be purified by site-specifically tagging them with adamantylammonium using the enzyme sortase A, followed by high-affinity binding with CB[7]-conjugated agarose beads and the recovery of the protein using a guest with a stronger affinity for CB[7]. The thermal and chemical stability of CB[7] beads and their scalability, recyclability and low cost may also make them advantageous for the manufacturing of biosimilars. The high-affinity and controllable host-guest interactions between cucurbit[7]uril and selected guests enables a versatile and scalable method for the purification of recombinant protein therapeutics.
- Keywords
- Biomolecules; Chemical stability; Monoclonal antibodies; Purification; Scalability; Biomolecular interactions; High affinity binding; Monoclonal antibody drugs; Protein denaturation; Protein therapeutics; Supramolecular host; Therapeutic protein; Thermal and chemical stabilities; Recombinant proteins
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/103984
- DOI
- 10.1038/s41551-020-0589-7
- ISSN
- 2157-846X
- Article Type
- Article
- Citation
- NATURE BIOMEDICAL ENGINEERING, 2020-07
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