BROWSE

Related Scientist

csc's photo.

csc
복잡계자기조립연구단
more info

ITEM VIEW & DOWNLOAD

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

DC Field Value Language
dc.contributor.authorJaeyeon An-
dc.contributor.authorSungwan Kim-
dc.contributor.authorAnnadka Shrinidhi-
dc.contributor.authorJunghyun Kim-
dc.contributor.authorHasanul Banna-
dc.contributor.authorGihyun Sung-
dc.contributor.authorKyeng Min Park-
dc.contributor.authorKimoon Kim-
dc.date.accessioned2021-01-11T05:30:06Z-
dc.date.accessioned2021-01-11T05:30:06Z-
dc.date.available2021-01-11T05:30:06Z-
dc.date.available2021-01-11T05:30:06Z-
dc.date.created2020-09-09-
dc.date.issued2020-11-
dc.identifier.issn2157-846X-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/9024-
dc.description.abstractEfficient 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.description.uri1-
dc.language영어-
dc.publisherNATURE PUBLISHING GROUP-
dc.titlePurification of protein therapeutics via high-affinity supramolecular host-guest interactions-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000550619800001-
dc.identifier.scopusid2-s2.0-85088953923-
dc.identifier.rimsid72981-
dc.contributor.affiliatedAuthorJaeyeon An-
dc.contributor.affiliatedAuthorSungwan Kim-
dc.contributor.affiliatedAuthorAnnadka Shrinidhi-
dc.contributor.affiliatedAuthorJunghyun Kim-
dc.contributor.affiliatedAuthorHasanul Banna-
dc.contributor.affiliatedAuthorGihyun Sung-
dc.contributor.affiliatedAuthorKyeng Min Park-
dc.contributor.affiliatedAuthorKimoon Kim-
dc.identifier.doi10.1038/s41551-020-0589-7-
dc.identifier.bibliographicCitationNATURE BIOMEDICAL ENGINEERING, v.4, no.11, pp.1044 - 1052-
dc.citation.titleNATURE BIOMEDICAL ENGINEERING-
dc.citation.volume4-
dc.citation.number11-
dc.citation.startPage1044-
dc.citation.endPage1052-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusANTIBODY-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusPAIR-
dc.subject.keywordPlusCUCURBITURIL-
dc.subject.keywordPlusIGG1-
dc.subject.keywordPlusTAG-
dc.subject.keywordAuthorANTIBODY-
dc.subject.keywordAuthorBINDING-
dc.subject.keywordAuthorPAIR-
dc.subject.keywordAuthorCUCURBITURIL-
dc.subject.keywordAuthorIGG1-
dc.subject.keywordAuthorTAG-
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > 1. Journal Papers (저널논문)
Files in This Item:
There are no files associated with this item.

qrcode

  • facebook

    twitter

  • Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse