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FibrilPaint1 is a 22mer peptide with exciting properties: i) FibrilPaint1 binds fibrils with nanomolar affinity; ii) it also binds to precursors, down to a size of only 4 layers; iii) it does not bind to monomers; iv) it is fluorescently labeled, which allows monitoring and localizing interactions; v) FibrilPaint1 recognizes various Tau fibrils, including patient-derived fibrils from AD, corticobasal degeneration (CBD), and frontotemporal dementia (FTD); vi) it also binds to fibrils from amyloids derived from Amyloid-\u03b2, \u03b1-synuclein, and huntingtin vii) FibrilPaint1 is selective for the amyloid state and does not have background binding to amorphous aggregates, blood serum, or cell lysate. In combination with flow-induced dispersion analysis (FIDA), a microfluidics technology, we determined the molecular size of amyloid fibrils with submicroliter sample volumes. This setup acts as a molecular ruler at layer resolution\u2014we determined Tau fibril length from 4 to 1100 layers in solution. This is an interesting parameter for molecular studies in dementia, with potential for diagnostic applications.<\/jats:p>","DOI":"10.1073\/pnas.2502847122","type":"journal-article","created":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T19:06:01Z","timestamp":1761591961000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":8,"title":["FibrilPaint to determine the length of Tau amyloids in fluids"],"prefix":"10.1073","volume":"122","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1991-3283","authenticated-orcid":false,"given":"J\u00falia","family":"Aragon\u00e8s Pedrola","sequence":"first","affiliation":[{"name":"Protein Chemistry of Disease, Department of Chemistry, Utrecht University","place":["Utrecht, The Netherlands"]},{"name":"Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University","place":["Utrecht, The Netherlands"]},{"name":"Science for Life, Utrecht University","place":["Utrecht, The Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fran\u00e7oise A.","family":"Dekker","sequence":"additional","affiliation":[{"name":"Protein Chemistry of Disease, Department of Chemistry, Utrecht University","place":["Utrecht, The Netherlands"]},{"name":"Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University","place":["Utrecht, The Netherlands"]},{"name":"Science for Life, Utrecht University","place":["Utrecht, The Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tommaso","family":"Garfagnini","sequence":"additional","affiliation":[{"name":"Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. 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