{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T17:29:33Z","timestamp":1791048573235,"version":"4.1.0"},"reference-count":30,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2009,9,9]],"date-time":"2009-09-09T00:00:00Z","timestamp":1252454400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2010,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Amyloid accumulation is associated with pathological conditions, including type II diabetes and Alzheimer's disease. Lipids influence amyloidogenesis and are themselves targets for amyloid\u2010mediated cell membrane disruption. Amyloid precursors are surface\u2010active, accumulating at hydrophobic\u2010hydrophilic interfaces\n                    <jats:italic>(e.g.,<\/jats:italic>\n                    air\u2010water), where their biophysical and kinetic behaviors differ from those in the bulk solution with significant and underappreciated consequences. Biophysical modeling predicted the probability and rate of \u03b2\u2010sheet amyloid dimer formation to be higher and faster at the air\u2010water interface (AWI) than in the bulk (by 14 and ~1500 times, respectively). Time\u2010course staining experiments with a typical amyloid dye verified our predictions by demonstrating that without AWI, islet amyloid polypeptide (IAPP) fibrilization was abolished or slowed, depending on the conditions. Our controls included undisturbed IAPP reactions, and we ascertained that the AWI removal process (technical or material) did not itself affect the reaction. Furthermore, we showed that the role of membranes in amy\u2010loidogenesis has been previously underestimated;in an\n                    <jats:italic>in vivo\u2010lke<\/jats:italic>\n                    situation (with no AWI), anionic liposomes (containing dioleoylphosphatidylglycerol) enhanced IAPP fibrilogenesis far more than described previously in conventional assay conditions (in the presence of an AWI). These findings have implications for the protein misfolding field and in assay design to target toxic protein aggregation.\u2014Jean, L., Lee, C. F., Lee, C., Shaw, M., Vaux, D. J. Competing discrete interfacial effects are critical for amyloidogenesis.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 24, 309\u2013317 (2010).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.09-137653","type":"journal-article","created":{"date-parts":[[2009,9,9]],"date-time":"2009-09-09T21:50:35Z","timestamp":1252533035000},"page":"309-317","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":51,"title":["Competing discrete interfacial effects are critical for amyloidogenesis"],"prefix":"10.1096","volume":"24","author":[{"given":"L\u00e9titia","family":"Jean","sequence":"first","affiliation":[{"name":"Sir William Dunn School of Pathology Department of Physics Clarendon Laboratory University of Oxford Oxford UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chiu Fan","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Physics Clarendon Laboratory University of Oxford Oxford UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chongsoo","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Physics Clarendon Laboratory University of Oxford Oxford UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Shaw","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology Department of Physics Clarendon Laboratory University of Oxford Oxford UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Vaux","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology Department of Physics Clarendon Laboratory University of Oxford Oxford UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,9,9]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C400260200"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0502066102"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M500997200"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2004.06.086"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi060579z"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1529\/biophysj.107.110635"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi971843e"},{"key":"e_1_2_6_9_1","doi-asserted-by":"crossref","first-page":"28551","DOI":"10.1016\/S0021-9258(19)61939-3","article-title":"Surfactant properties of Alzheimer's A\u03b2 peptides and the mechanism of amyloid aggregation","volume":"269","author":"Soreghan B.","year":"1994","journal-title":"J. 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