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Fast and Efficient Fc-Specific Photoaffinity Labeling To Produce Antibody-DNA Conjugates
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.ORCID iD: 0000-0002-6552-8426
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Gene Technology. KTH, Centres, Science for Life Laboratory, SciLifeLab.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Gene Technology. KTH, Centres, Science for Life Laboratory, SciLifeLab.ORCID iD: 0000-0002-3174-2096
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.ORCID iD: 0000-0003-4334-9360
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2019 (English)In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 30, no 11, p. 2790-2798Article in journal (Refereed) Published
Abstract [en]

Antibody DNA conjugates are powerful tools for DNA-assisted protein analysis. Growing usage of these methods demands efficient production of high-quality conjugates. We developed an easy and fast synthesis route yielding covalent antibody-DNA conjugates with a defined conjugation site and low batch-to-batch variability. We utilize the Z domain from protein A, containing the unnatural amino acid 4-benzoylphenylalanine (BPA) for photoaffinity labeling of the antibodies' Fc region. Z(xBPA) domains are C-terminally modified with triple-glycine (G(3))-modified DNA-oligonucleotides enzymatic Sortase A coupling. We reliable modification of the most commonly used IgG's. To prove our conjugates' functionality, we detected antibody-antigen binding events in an assay called Droplet Barcode Sequencing for Protein analysis (DBS-Pro). It confirms not only retained functionality for both conjugate parts but also the potential of using DBS-Pro for quantifying protein abundances. As intermediates are easily storable and our approach is modular, it offers a convenient strategy for screening various antibody-DNA conjugates using the same starting material.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2019. Vol. 30, no 11, p. 2790-2798
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-265445DOI: 10.1021/acs.bioconjchem.9b00548ISI: 000499743100008PubMedID: 31609586Scopus ID: 2-s2.0-85074441977OAI: oai:DiVA.org:kth-265445DiVA, id: diva2:1377652
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20191212

Available from: 2019-12-12 Created: 2019-12-12 Last updated: 2020-01-02Bibliographically approved

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Stiller, ChristianeAghelpasand, HoomanFrick, TobiasWesterlund, KristinaAhmadian, AfshinEriksson Karlström, Amelie

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Stiller, ChristianeAghelpasand, HoomanFrick, TobiasWesterlund, KristinaAhmadian, AfshinEriksson Karlström, Amelie
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Bioconjugate chemistry
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