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In this study, we introduce a new approach to monitor site-specific conformational transitions that occur during infectious prion formation. The method relies on genetically encoded substitution of a fluorescent, environmentally sensitive noncanonical amino acid, l-(7-hydroxycoumarin-4-yl)ethylglycine (7-HCAA), into recombinant PrP substrate molecules, allowing real-time monitoring of structural changes in high-efficiency in vitro PrPSc conversion reactions. As proof of principle, we show that the W99 7-HCAA recPrP substrate efficiently propagates two different PrPSc conformers (infectious cofactor PrPSc and noninfectious protein-only PrPSc). Bioassays in knock-in mice expressing bank vole PrP confirm that W99 7-HCAA cofactor PrPSc produced by serial propagation is infectious, causing scrapie with an incubation period and neuropathological profile like those induced by wild-type cofactor PrPSc. Marked differences in fluorescence intensity were observed between native, misfolded, and denatured states of W99 7-HCAA PrP, confirming that 7-HCAA reports on local changes in PrP conformation. Together, these findings establish 7-HCAA as a site-specific and sensitive probe of local PrP conformation. Moreover, the results suggest a new strategy for studying conformational dynamics in amyloid-forming proteins.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00351","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T01:24:26Z","timestamp":1788225866000},"page":"2841-2850","source":"Crossref","is-referenced-by-count":0,"title":["A Unique Platform\nto Study the Dynamic Process of\nPrion Formation"],"prefix":"10.1021","volume":"65","author":[{"given":"Jessica","family":"de Alcantara Ferreira","sequence":"first","affiliation":[{"name":"Geisel School of Medicine at Dartmouth , , , ,","place":["Hanover, New Hampshire, United States, 03755"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel J.","family":"Walsh","sequence":"additional","affiliation":[{"name":"Geisel School of Medicine at Dartmouth , , , ,","place":["Hanover, New Hampshire, United States, 03755"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evelyn","family":"Turnbaugh","sequence":"additional","affiliation":[{"name":"Geisel School of Medicine at Dartmouth , , , ,","place":["Hanover, New Hampshire, United States, 03755"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2017-1846","authenticated-orcid":true,"given":"Jeremy H.","family":"Mills","sequence":"additional","affiliation":[{"name":"Arizona State University , , ,","place":["Tempe, Arizona, United States, 85287"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9060-4550","authenticated-orcid":true,"given":"Surachai","family":"Supattapone","sequence":"additional","affiliation":[{"name":"Geisel School of Medicine at Dartmouth , , , ,","place":["Hanover, New Hampshire, United States, 03755"]},{"name":"Geisel School of Medicine at Dartmouth , , , ,","place":["Hanover, New Hampshire, United States, 03755"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,25]]},"reference":[{"key":"2026091508065733200_cit1","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous\ninfectious particles cause scrapie","volume":"216","author":"Prusiner","year":"1982","journal-title":"Science"},{"key":"2026091508065733200_cit2","doi-asserted-by":"publisher","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc.\nNatl. 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