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Protein engineering allows for mild affinity-based elution of therapeutic antibodies
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Technology. (Hober lab)ORCID iD: 0000-0002-4751-2519
Lund University.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Technology. (Hober lab)
KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.ORCID iD: 0000-0002-6104-6446
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2018 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 430, no 18, p. 3427-3438Article in journal (Refereed) Published
Abstract [en]

Presented here is an engineered protein domain, based on Protein A, that displays a calcium-dependent binding to antibodies. This protein, ZCa, is shown to efficiently function as an affinity ligand for mild purification of antibodies through elution with ethylenediaminetetraacetic acid. Antibodies are commonly used tools in the area of biological sciences and as therapeutics, and the most commonly used approach for antibody purification is based on Protein A using acidic elution. Although this affinity-based method is robust and efficient, the requirement for low pH elution can be detrimental to the protein being purified. By introducing a calcium-binding loop in the Protein A-derived Z domain, it has been re-engineered to provide efficient antibody purification under mild conditions. Through comprehensive analyses of the domain as well as the ZCa–Fc complex, the features of this domain are well understood. This novel protein domain provides a very valuable tool for effective and gentle antibody and Fc-fusion protein purification

Place, publisher, year, edition, pages
Elsevier, 2018. Vol. 430, no 18, p. 3427-3438
Keywords [en]
antibody purification, calcium-dependent binding, Protein A, protein engineering, Z domain
National Category
Pharmaceutical Biotechnology
Research subject
Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-238507DOI: 10.1016/j.jmb.2018.06.004ISI: 000444668100025Scopus ID: 2-s2.0-85048734234OAI: oai:DiVA.org:kth-238507DiVA, id: diva2:1260591
Funder
VINNOVA
Note

QC 20181130

Available from: 2018-11-04 Created: 2018-11-04 Last updated: 2019-01-28Bibliographically approved

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Kanje, SaraScheffel, JuliaNilvebrant, JohanHober, Sophia

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