{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T18:17:27Z","timestamp":1759342647305},"reference-count":25,"publisher":"Bentham Science Publishers Ltd.","issue":"5","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["PPL"],"published-print":{"date-parts":[[2019,5,29]]},"abstract":"<jats:sec>\n<jats:title>Background:<\/jats:title>\n<jats:p>The structural transition of aggregating Abeta peptides is the key event in\nthe progression of Alzheimer\u2019s Disease (AD).<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Objective:<\/jats:title>\n<jats:p> In the present work, the structural modifications of toxic A\u03b225-35 and the scrambled\nA\u03b235-25 were studied in Trifluoroethanol (TFE) and in aqueous SDS micelles.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Methods:<\/jats:title>\n<jats:p>Using CD spectroscopic investigations, the conformational transition of A\u03b225-35 and\nA\u03b235-25 peptides were determined in different membrane mimicking environments such as TFE and\nSDS. An interval scan CD of the peptides on evaporation of TFE was performed. TFE titrations\nwere carried out to investigate the intrinsic ability of the structural conformations of peptides.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Results:<\/jats:title>\n<jats:p>We show by spectroscopic evidence that A\u03b225-35 prefers beta sheet structures upon\nincreasing TFE concentrations. On the other hand, the non-toxic scrambled A\u03b235-25 peptide only\nundergoes a transition from random coil to \u03b1-helix conformation with increasing TFE. In the\ninterval scan studies, A\u03b225-35 did not show any structural transitions, whereas A\u03b235-25 showed\ntransition from \u03b1-helix to \u03b2-sheet conformation. In membrane simulating aqueous SDS micelles,\nA\u03b225-35 showed a transition from random coil to \u03b1-helix while A\u03b235-25 underwent transition from\nrandom coil to \u03b2-sheet conformation.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Conclusion:<\/jats:title>\n<jats:p> Overall, the current results seek new insights into the structural properties of\namyloidogenic and the truncated sequence in membrane mimicking solvents.<\/jats:p>\n<\/jats:sec>","DOI":"10.2174\/0929866526666190228122849","type":"journal-article","created":{"date-parts":[[2019,3,6]],"date-time":"2019-03-06T08:11:17Z","timestamp":1551859877000},"page":"386-390","update-policy":"http:\/\/dx.doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Conformational Preferences of A\u03b225-35 and A\u03b235-25 in Membrane Mimicking Environments"],"prefix":"10.2174","volume":"26","author":[{"given":"Dhandayuthapani","family":"Sambasivam","sequence":"first","affiliation":[{"name":"Bioorganic Chemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Senthilkumar","family":"Sivanesan","sequence":"additional","affiliation":[{"name":"Bioorganic Chemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sayeeda","family":"Sultana","sequence":"additional","affiliation":[{"name":"Department of Chemistry, St Peter's Institute of Higher Education and Research, Chennai-600054, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jayakumar","family":"Rajadas","sequence":"additional","affiliation":[{"name":"Bioorganic Chemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"965","reference":[{"key":"ref=1","first-page":"66-71","volume":"15","author":"Cuello A.C.","year":"2005","unstructured":".  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