{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T11:17:24Z","timestamp":1788347844842,"version":"build-2803163510"},"reference-count":68,"publisher":"American Chemical Society (ACS)","issue":"9","license":[{"start":{"date-parts":[[2018,9,24]],"date-time":"2018-09-24T00:00:00Z","timestamp":1537747200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,9,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Understanding protein aggregation is of utmost importance as it is responsible for causing several neurodegenerative diseases and one of the serious impediments in large-scale biopharmaceutical production. The prion protein is responsible for pathological states in fatal transmissible spongiform conditions, such as Creutzfeldt\u2013Jakob disease and bovine spongiform encephalopathy. The peptide fragment 178\u2013191 of Syrian hamster prion protein is known to be amyloidogenic. Here, we identified the fragment 179CVNITV184 as an aggregation-prone fragment in sheep prion protein. This fragment is conserved sequence among sheep and Syrian hamster prion protein and also falls in the previously identified amyloidogenic sequence. The mechanistic details of the aggregation behavior are analyzed in three different concentrations of urea, arginine, and ethanol. Urea and arginine are found to be aggregation suppressors, but ethanol enhances the protein aggregation through \u03b2-sheet formation. We have also analyzed the influence of these osmolyte on water dynamics in the presence of the octamer of this aggregation-prone fragment and correlated this water dynamics with the aggregation behavior of the octamer.<\/jats:p>","DOI":"10.1021\/acsomega.8b00875","type":"journal-article","created":{"date-parts":[[2018,9,24]],"date-time":"2018-09-24T12:53:59Z","timestamp":1537793639000},"page":"11727-11741","source":"Crossref","is-referenced-by-count":19,"title":["Effect of Urea, Arginine, and Ethanol Concentration\non Aggregation of 179CVNITV184 Fragment of Sheep\nPrion Protein"],"prefix":"10.1021","volume":"3","author":[{"given":"Ishrat","family":"Jahan","sequence":"first","affiliation":[{"name":"Aligarh Muslim University , , , ,","place":["Aligarh, U.P., India, 202002"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6478-9835","authenticated-orcid":true,"given":"Shahid M.","family":"Nayeem","sequence":"additional","affiliation":[{"name":"Aligarh Muslim University , , , ,","place":["Aligarh, U.P., India, 202002"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2018,9,24]]},"reference":[{"key":"2026090206582659400_cit1","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1023\/b:pham.0000029275.41323.a6","article-title":"Structure-immunogenicity\nrelationships of therapeutic proteins","volume":"21","author":"Hermeling","year":"2004","journal-title":"Pharm.\nRes."},{"key":"2026090206582659400_cit2","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1038\/383685a0","article-title":"Molecular\nanalysis of prion strain variation and the aetiology of \u2018new\nvariant\u2019 CJD","volume":"383","author":"Collinge","year":"1996","journal-title":"Nature"},{"key":"2026090206582659400_cit3","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1038\/38925","article-title":"The same prion strain\ncauses vCJD and BSE","volume":"389","author":"Hill","year":"1997","journal-title":"Nature"},{"key":"2026090206582659400_cit4","doi-asserted-by":"publisher","first-page":"498","DOI":"10.1038\/39057","article-title":"Transmissions to mice indicate that \u2018new variant\u2019\nCJD is caused by the BSE agent","volume":"389","author":"Bruce","year":"1997","journal-title":"Nature"},{"key":"2026090206582659400_cit5","doi-asserted-by":"publisher","first-page":"6358","DOI":"10.1093\/emboj\/cdf653","article-title":"BSE prions propagate as either variant\nCJD-like or sporadic CJD-like prion strains in transgenic mice expressing\nhuman prion protein","volume":"21","author":"Asante","year":"2002","journal-title":"EMBO J."},{"key":"2026090206582659400_cit6","doi-asserted-by":"publisher","first-page":"530","DOI":"10.1126\/science.7909169","article-title":"Structural clues to prion replication","volume":"264","author":"Cohen","year":"1994","journal-title":"Science"},{"key":"2026090206582659400_cit7","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1146\/annurev.biochem.67.1.793","article-title":"Pathologic conformations\nof prion proteins","volume":"67","author":"Cohen","year":"1998","journal-title":"Annu. 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