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Here, we report a phage display-based sequential development path of such antibodies. The strategy goes from initial lead identification through in silico informed CDR engineering in combination with framework engineering for affinity and thermostability optimization, respectively. The strategy allowed the identification of HLA-DQ2.5 gluten peptide-specific TCR-like antibodies with low picomolar affinity. Our method outlines an efficient and general method for development of this promising class of antibodies, which should facilitate their utility including translation to human therapy.<\/jats:p>","DOI":"10.1093\/protein\/gzac005","type":"journal-article","created":{"date-parts":[[2022,7,25]],"date-time":"2022-07-25T01:08:58Z","timestamp":1658711338000},"source":"Crossref","is-referenced-by-count":2,"title":["Affinity maturation of TCR-like antibodies using phage display guided by structural modeling"],"prefix":"10.1093","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3469-5686","authenticated-orcid":false,"given":"Rahel","family":"Frick","sequence":"first","affiliation":[{"name":"Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital , Sognsvannsveien 20, 0372 Oslo, Norway"},{"name":"Centre for Immune Regulation and Department of Biosciences, University of Oslo , Blindernveien 31, 0371 Oslo, Norway"},{"name":"Department of Chemical and Biomolecular Engineering, Johns Hopkins University , 3400 N. 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Charles Street, Baltimore, MD 21218, USA"},{"name":"Department of Chemical and Biomolecular Engineering and Institute of NanoBioTechnology, Johns Hopkins University , 3400 N. 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