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Purification of protein therapeutics via high-affinity supramolecular host-guest interactions

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Title
Purification of protein therapeutics via high-affinity supramolecular host-guest interactions
Author(s)
Jaeyeon An; Sungwan Kim; Annadka Shrinidhi; Junghyun Kim; Hasanul Banna; Gihyun Sung; Kyeng Min Park; Kimoon Kim
Publication Date
2020-11
Journal
NATURE BIOMEDICAL ENGINEERING, v.4, no.11, pp.1044 - 1052
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
URI
https://pr.ibs.re.kr/handle/8788114/9024
DOI
10.1038/s41551-020-0589-7
ISSN
2157-846X
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > 1. Journal Papers (저널논문)
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