{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:54:55Z","timestamp":1790776495266,"version":"4.1.0"},"reference-count":68,"publisher":"Wiley","issue":"64","license":[{"start":{"date-parts":[[2020,10,7]],"date-time":"2020-10-07T00:00:00Z","timestamp":1602028800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Chemistry A European J"],"published-print":{"date-parts":[[2020,11,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Type\u20052 diabetes (T2D) and Alzheimer's disease (AD) belong to the 10 deadliest diseases and are sorely lacking in effective treatments. Both pathologies are part of the degenerative disorders named amyloidoses, which involve the misfolding and the aggregation of amyloid peptides, hIAPP for T2D and A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    for AD. While hIAPP and A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    inhibitors have been essentially designed to target \u03b2\u2010sheet\u2010rich structures composing the toxic amyloid oligomers and fibrils of these peptides, the strategy aiming at trapping the non\u2010toxic monomers in their helical native conformation has been rarely explored. We report herein the first example of helical foldamers as dual inhibitors of hIAPP and A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation and able to preserve the monomeric species of both amyloid peptides. A foldamer composed of 4\u2010amino(methyl)\u20101,3\u2010thiazole\u20105\u2010carboxylic acid (ATC) units, adopting a 9\u2010helix structure reminiscent of 3\n                    <jats:sub>10<\/jats:sub>\n                    helix, was remarkable as demonstrated by biophysical assays combining thioflavin\u2010T fluorescence, transmission electronic microscopy, capillary electrophoresis and mass spectrometry.\n                  <\/jats:p>","DOI":"10.1002\/chem.202001716","type":"journal-article","created":{"date-parts":[[2020,6,15]],"date-time":"2020-06-15T13:24:50Z","timestamp":1592227490000},"page":"14612-14622","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Helical \u03b3\u2010Peptide Foldamers as Dual Inhibitors of Amyloid\u2010\u03b2 Peptide and Islet Amyloid Polypeptide Oligomerization and Fibrillization"],"prefix":"10.1002","volume":"26","author":[{"given":"Julia","family":"Kaffy","sequence":"first","affiliation":[{"name":"Universit\u00e9 Paris-Saclay CNRS BioCIS  92290 Ch\u00e2tenay-Malabry France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Corentin","family":"Berardet","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay CNRS BioCIS  92290 Ch\u00e2tenay-Malabry France"},{"name":"Universit\u00e9 Paris Saclay CNRS Institut Galien de Paris Sud  92290 Ch\u00e2tenay-Malabry France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lo\u00efc","family":"Mathieu","sequence":"additional","affiliation":[{"name":"Institut des Biomol\u00e9cules Max Mousseron UMR 5247 CNRS Universit\u00e9 de Montpellier-CNRS-ENSCM, UMR 5247 UFR des Sciences Pharmaceutiques et Biologiques  15 Avenue Charles Flahault 34093 Montpellier Cedex 5 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baptiste","family":"Legrand","sequence":"additional","affiliation":[{"name":"Institut des Biomol\u00e9cules Max Mousseron UMR 5247 CNRS Universit\u00e9 de Montpellier-CNRS-ENSCM, UMR 5247 UFR des Sciences Pharmaceutiques et Biologiques  15 Avenue Charles Flahault 34093 Montpellier Cedex 5 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Myriam","family":"Taverna","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris Saclay CNRS Institut Galien de Paris Sud  92290 Ch\u00e2tenay-Malabry France"},{"name":"Institut Universitaire de France  1, rue Descartes 75231 Paris Cedex 05 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fr\u00e9d\u00e9ric","family":"Halgand","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay CNRS Institut de Chimie Physique  91405 Orsay France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillaume","family":"Van Der Rest","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay CNRS Institut de Chimie Physique  91405 Orsay France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ludovic T.","family":"Maillard","sequence":"additional","affiliation":[{"name":"Institut des Biomol\u00e9cules Max Mousseron UMR 5247 CNRS Universit\u00e9 de Montpellier-CNRS-ENSCM, UMR 5247 UFR des Sciences Pharmaceutiques et Biologiques  15 Avenue Charles Flahault 34093 Montpellier Cedex 5 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2118-7324","authenticated-orcid":false,"given":"Sandrine","family":"Ongeri","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay CNRS BioCIS  92290 Ch\u00e2tenay-Malabry France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,10,7]]},"reference":[{"key":"e_1_2_7_1_1","doi-asserted-by":"publisher","DOI":"10.3389\/fendo.2017.00006"},{"key":"e_1_2_7_2_1","unstructured":"World Alzheimer Reports|Alzheimer's Disease International can be found underhttps:\/\/www.alz.co.uk\/research\/world-report 2018."},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neurobiolaging.2005.09.014"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbadis.2008.12.003"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11892-014-0476-2"},{"key":"e_1_2_7_6_1","first-page":"41","volume":"7","author":"Song M. 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