{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,3]],"date-time":"2025-12-03T17:38:57Z","timestamp":1764783537290},"reference-count":51,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,11,15]]},"abstract":"<jats:p>Amyloid formation is a hallmark of protein misfolding diseases (e.g. Type\u00a0II diabetes mellitus). The energetically unfavourable nucleation step of amyloidogenesis can be accelerated by seeding, during which pre-formed aggregates act as templates for monomer recruitment. Hydrophobic\u2013hydrophilic interfaces [e.g. AWI (air\u2013water interface)] can also catalyse amyloidogenesis due to the surfactant properties of amyloidogenic polypeptides. Using thioflavin T fluorescence and electron microscopy, we demonstrate that the outcome of seeding on human islet amyloid polypeptide amyloidogenesis is dependent upon whether the AWI is present or absent and is dictated by seed type. Seeding significantly inhibits (with AWI) or promotes (without AWI) plateau height compared with seedless controls; with short fibrils being more efficient seeds than their longer counterparts. Moreover, promotion of nucleation by increasing monomer concentrations can only be observed in the absence of an AWI. Using biophysical modelling, we suggest that a possible explanation for our results may reside in lateral interactions between seeds and monomers determining the fibril mass formed in seeded reactions at steady-state. Our results suggest that in\u00a0vivo hydrophobic\u2013hydrophilic interfaces (e.g. the presence of membranes and their turnover rate) may dictate the outcome of seeding during amyloidogenesis and that factors affecting the size of the pre-aggregate may be important.<\/jats:p>","DOI":"10.1042\/bj20130605","type":"journal-article","created":{"date-parts":[[2013,9,11]],"date-time":"2013-09-11T06:38:52Z","timestamp":1378881532000},"page":"67-80","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["The air\u2013water interface determines the outcome of seeding during amyloidogenesis"],"prefix":"10.1042","volume":"456","author":[{"given":"Ben\u00a0J.","family":"Trigg","sequence":"first","affiliation":[{"name":"Department of Zoology, University of Oxford, Oxford OX1 3PS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chiu\u00a0Fan","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Imperial College London, South Kensington Campus, London SW7 2AZ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David\u00a0J.","family":"Vaux","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L\u00e9titia","family":"Jean","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2013,10,24]]},"reference":[{"key":"2021112215481519800_B1","doi-asserted-by":"crossref","first-page":"101","DOI":"10.3109\/13506129.2010.526812","article-title":"Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis","volume":"17","author":"Sipe","year":"2010","journal-title":"Amyloid"},{"key":"2021112215481519800_B2","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","author":"Stefani","year":"2003","journal-title":"J. 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