ArticleProtein science : a publication of the Protein Society2025
Screening de novo designed protein binders in unpurified lysate using flow induced dispersion analysis.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins.Protein science : a publication of the Protein Society · 2026Article
- Sequence determinants of the hypomobility of intrinsically disordered proteins in SDS-PAGE.Protein science : a publication of the Protein Society · 2026Article
- Flow-induced dispersion analysis for probing cyclodextrin-guest binding interactions.European biophysics journal : EBJ · 2026Article
- Optimization of Recombinant Human Interferon-Gamma Expression and Purification inBiologics : targets & therapy · 2026Article
- Screening de novo designed protein binders in unpurified lysate using flow induced dispersion analysis.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
7 authors.
Funding
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. Subsequent titration experiments show micromolar affinities for ALFA-tag binders and nanomolar affinities for GK domain binders. The lack of immobilization, the minimal sample volume, and the compatibility with complex biological samples position FIDA as a valuable tool for the screening and characterization of computationally generated protein binders.
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Registered trials
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