{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pinheiro F"],"funding":["Danmarks Grundforskningsfond","Danmarks Frie Forskningsfond","Lundbeck Foundation"],"pagination":["e70286"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12432402"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(10)"],"pubmed_abstract":["Computational protein design can create binders against targets of interest, but identifying binders with sufficient affinity still requires biochemical screening of many designs. In this work, we test flow-induced dispersion analysis (FIDA) as a method for screening binders in a time and cost-effective manner. FIDA uses Taylor dispersion analysis to determine the hydrodynamic radius of fluorescently labeled biomolecules and their complexes. Here, we use FIDA to assess the binding of RFdiffusion-designed protein binders against the small helical peptide ALFA-tag and the guanylate kinase (GK) domain of PSD-95. Successful binders can be identified in a single measurement using heat-treated bacterial lysates, allowing rapid identification of binders with high affinity and thermostability. Sub"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Screening de novo designed protein binders in unpurified lysate using flow induced dispersion analysis."],"pmcid":["PMC12432402"],"funding_grant_id":["026-00069B","DNRF133","R449-2023-1396"],"pubmed_authors":["Nowak JS","Pheasant EC","Zueva E","Lampinen V","Kjaergaard M","Pinheiro F","Grene IK"],"additional_accession":[]},"is_claimable":false,"name":"Screening de novo designed protein binders in unpurified lysate using flow induced dispersion analysis.","description":"Computational protein design can create binders against targets of interest, but identifying binders with sufficient affinity still requires biochemical screening of many designs. In this work, we test flow-induced dispersion analysis (FIDA) as a method for screening binders in a time and cost-effective manner. FIDA uses Taylor dispersion analysis to determine the hydrodynamic radius of fluorescently labeled biomolecules and their complexes. Here, we use FIDA to assess the binding of RFdiffusion-designed protein binders against the small helical peptide ALFA-tag and the guanylate kinase (GK) domain of PSD-95. Successful binders can be identified in a single measurement using heat-treated bacterial lysates, allowing rapid identification of binders with high affinity and thermostability. Sub","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-03T03:03:25.659Z","creation":"2026-04-23T03:13:14.685Z"},"accession":"S-EPMC12432402","cross_references":{"pubmed":["40944422"],"doi":["10.1002/pro.70286"]}}