DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jaeyeon An | - |
dc.contributor.author | Sungwan Kim | - |
dc.contributor.author | Annadka Shrinidhi | - |
dc.contributor.author | Junghyun Kim | - |
dc.contributor.author | Hasanul Banna | - |
dc.contributor.author | Gihyun Sung | - |
dc.contributor.author | Kyeng Min Park | - |
dc.contributor.author | Kimoon Kim | - |
dc.date.accessioned | 2020-08-19T09:50:20Z | - |
dc.date.available | 2020-08-19T09:50:20Z | - |
dc.date.created | 2020-07-30 | - |
dc.date.issued | 2020-07 | - |
dc.identifier.issn | 2157-846X | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/103984 | - |
dc.description.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. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.relation.isPartOf | NATURE BIOMEDICAL ENGINEERING | - |
dc.subject | Biomolecules | - |
dc.subject | Chemical stability | - |
dc.subject | Monoclonal antibodies | - |
dc.subject | Purification | - |
dc.subject | Scalability | - |
dc.subject | Biomolecular interactions | - |
dc.subject | High affinity binding | - |
dc.subject | Monoclonal antibody drugs | - |
dc.subject | Protein denaturation | - |
dc.subject | Protein therapeutics | - |
dc.subject | Supramolecular host | - |
dc.subject | Therapeutic protein | - |
dc.subject | Thermal and chemical stabilities | - |
dc.subject | Recombinant proteins | - |
dc.title | Purification of protein therapeutics via high-affinity supramolecular host-guest interactions | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s41551-020-0589-7 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | NATURE BIOMEDICAL ENGINEERING | - |
dc.identifier.wosid | 000550619800001 | - |
dc.citation.title | NATURE BIOMEDICAL ENGINEERING | - |
dc.contributor.affiliatedAuthor | Jaeyeon An | - |
dc.contributor.affiliatedAuthor | Sungwan Kim | - |
dc.contributor.affiliatedAuthor | Hasanul Banna | - |
dc.contributor.affiliatedAuthor | Gihyun Sung | - |
dc.contributor.affiliatedAuthor | Kimoon Kim | - |
dc.identifier.scopusid | 2-s2.0-85088953923 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article; Early Access | - |
dc.subject.keywordPlus | ANTIBODY | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | PAIR | - |
dc.subject.keywordPlus | CUCURBITURIL | - |
dc.subject.keywordPlus | IGG1 | - |
dc.subject.keywordPlus | TAG | - |
dc.relation.journalWebOfScienceCategory | Engineering, Biomedical | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Engineering | - |
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