{"entity": "publication", "iuid": "08599c1d974b4557943924c04c7fa1c5", "timestamp": "2026-09-28T11:20:08.739Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/08599c1d974b4557943924c04c7fa1c5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/08599c1d974b4557943924c04c7fa1c5"}}, "title": "Fast and Efficient Fc-Specific Photoaffinity Labeling To Produce Antibody-DNA Conjugates.", "authors": [{"family": "Stiller", "given": "Christiane", "initials": "C", "orcid": "0000-0002-6552-8426", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9edd629c5dac43728165118ddd7bc5b5.json"}}, {"family": "Aghelpasand", "given": "Hooman", "initials": "H"}, {"family": "Frick", "given": "Tobias", "initials": "T"}, {"family": "Westerlund", "given": "Kristina", "initials": "K"}, {"family": "Ahmadian", "given": "Afshin", "initials": "A"}, {"family": "Karlstr\u00f6m", "given": "Amelie Eriksson", "initials": "AE", "orcid": "0000-0002-0695-5188", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/084ac56a883542f0b79ac6f63a9d6b1d.json"}}], "type": "journal article", "published": "2019-11-20", "journal": {"title": "Bioconjug. Chem.", "issn": "1520-4812", "volume": "30", "issue": "11", "pages": "2790-2798", "issn-l": "1043-1802"}, "abstract": "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 (G3)-modified DNA-oligonucleotides via enzymatic Sortase A coupling. We show 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.", "doi": "10.1021/acs.bioconjchem.9b00548", "pmid": "31609586", "labels": [], "xrefs": [], "notes": [], "created": "2026-09-23T10:13:40.432Z", "modified": "2026-09-23T10:52:05.413Z"}