{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,28]],"date-time":"2025-09-28T12:48:37Z","timestamp":1759063717292},"reference-count":44,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":2133,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>At the heart of the pathogenesis of transmissible spongiform encephalopathies (TSEs), such as BSE, scrapie, and Creutzfeldt\u2013Jakob disease, lies a poorly understood structural rearrangement of PrP, an abundant glycoprotein of the nervous and lymphoid systems. The normal form (PrP<jats:sup>C<\/jats:sup>), rich in \u03b1\u2010helix, converts into an aberrant \u03b2\u2010sheet\u2010dominated form (PrP<jats:sup>Sc<\/jats:sup>), which seems to be at the center of the pathotoxic symptoms observed in TSEs. To understand this process better at a molecular level, we have studied the interactions between different peptides derived from bovine PrP and their structural significance. We show that two unstructured peptides derived from the central region of bovine PrP, residues 115\u2013133 and 140\u2013152, respectively, interact stoichiometrically under physiological conditions to generate \u03b2\u2010sheet\u2010dominated fibrils. However, when both peptides are incubated in the presence of a third peptide derived from an adjoining \u03b1\u2010helical region (residues 153\u2013169), the formation of \u03b2\u2010sheet\u2010rich fibrils is abolished. These data indicate that native PrP<jats:sup>C<\/jats:sup> helix 1 might inhibit the strong intrinsic \u03b2\u2010sheet\u2010forming propensity of sequences immediately N\u2010terminal to the globular core of PrP<jats:sup>C<\/jats:sup>, by keeping in place intrachain interactions that would prevent these amyloidogenic regions from triggering aggregation. Moreover, these results indicate new ways in which PrP<jats:sup>Sc<\/jats:sup> formation could be prevented.<\/jats:p>","DOI":"10.1110\/ps.0236703","type":"journal-article","created":{"date-parts":[[2003,2,18]],"date-time":"2003-02-18T23:47:24Z","timestamp":1045612044000},"page":"600-608","source":"Crossref","is-referenced-by-count":13,"title":["Competing intrachain interactions regulate the formation of \u03b2\u2010sheet fibrils in bovine PrP peptides"],"prefix":"10.1002","volume":"12","author":[{"given":"Abdessamad","family":"Tahiri\u2010Alaoui","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mario","family":"Bouchard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jes\u00fas","family":"Zurdo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"William","family":"James","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.14.7182"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi9923353"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C100180200"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111402200"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/385787a0"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1006\/mcne.1999.0796"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1038\/37783"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/416507a"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.7.3590"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.67.1.793"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(99)01445-0"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.25.13452"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/362543a0"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02815218"},{"key":"e_1_2_7_16_1","doi-asserted-by":"crossref","first-page":"10940","DOI":"10.1073\/pnas.89.22.10940","article-title":"Predicted \u03b1\u2010helical regions of the prion protein when synthesized as peptides form amyloid","volume":"89","author":"Gasset M.","year":"1992","journal-title":"Proc. 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