{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T05:58:56Z","timestamp":1791093536685,"version":"4.1.0"},"reference-count":39,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":2648,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2001,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We previously demonstrated that a \u03b2\u2010hairpin peptide, termed BH<jats:sup>9\u201310<\/jats:sup>, derived from a single\u2010layer \u03b2\u2010sheet of <jats:italic>Borrelia<\/jats:italic> OspA protein, formed a native\u2010like \u03b2\u2010turn in trifluoroethanol (TFE) solution, and it assembled into amyloid\u2010like fibrils at higher TFE concentrations. This peptide is highly charged, and fibrillization of such a hydrophilic peptide is quite unusual. In this study, we designed a circularly permutated peptide of BH<jats:sup>9\u201310<\/jats:sup>, termed BH<jats:sup>10\u20139<\/jats:sup>. When folded into their respective \u03b2\u2010hairpin structures found in OspA, these peptides would have identical cross\u2010strand interactions but different turns connecting the strands. NMR study revealed that BH<jats:sup>10\u20139<\/jats:sup> had little propensity to form a turn structure both in aqueous and TFE solutions. At higher TFE concentration, BH<jats:sup>10\u20139<\/jats:sup> precipitated with a concomitant \u03b1\u2010to\u2010\u03b2 conformational conversion, in a similar manner to the BH<jats:sup>9\u201310<\/jats:sup> fibrillization. However, the BH<jats:sup>10\u20139<\/jats:sup> precipitates were nonfibrillar aggregation. The precipitation kinetics of BH<jats:sup>10\u20139<\/jats:sup> was exponential, consistent with a first\u2010order molecular assembly reaction, while the fibrillization of BH<jats:sup>9\u201310<\/jats:sup> showed sigmoidal kinetics, indicative of a two\u2010step reaction consisting of nucleation and molecular assembly. The correlation between native\u2010like turn formation and fibrillization of our peptide system strongly suggests that BH<jats:sup>9\u201310<\/jats:sup> adopts a native\u2010like \u03b2\u2010hairpin conformation in the fibrils. Remarkably, seeding with the preformed BH<jats:sup>10\u20139<\/jats:sup> precipitates changed the two\u2010step BH<jats:sup>9\u201310<\/jats:sup> fibrillization to a one\u2010step molecular assembly reaction, and disrupted the BH<jats:sup>9\u201310<\/jats:sup> fibril structure, indicating interactions between the BH<jats:sup>10\u20139<\/jats:sup> aggregates and the BH<jats:sup>9\u201310<\/jats:sup> peptide. Our results suggest that, in these peptides, cross\u2010strand interactions are the driving force for molecular assembly, and turn formation limits modes of peptide assembly.<\/jats:p>","DOI":"10.1110\/ps.15901","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T23:59:58Z","timestamp":1027727998000},"page":"2083-2092","source":"Crossref","is-referenced-by-count":19,"title":["The roles of turn formation and cross\u2010strand interactions in fibrillization of peptides derived from the OspA single\u2010layer \u03b2\u2010sheet"],"prefix":"10.1002","volume":"10","author":[{"given":"Satoshi","family":"Ohnishi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akiko","family":"Koide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shohei","family":"Koide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF01875320"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(83)90226-3"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.3514"},{"key":"e_1_2_8_5_1","first-page":"905","article-title":"Crystallography and NMR system: A new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger 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