{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,5]],"date-time":"2026-01-05T22:15:40Z","timestamp":1767651340435,"version":"build-2065373602"},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2013,1,9]],"date-time":"2013-01-09T00:00:00Z","timestamp":1357689600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Chemistry \u0097 An Asian Journal"],"published-print":{"date-parts":[[2013,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amyloid peptides, A\u03b21\u201340 and A\u03b21\u201342, represent major molecular targets to develop potential drugs and diagnostic tools for Alzheimer\u2019s Disease (AD). In fact, oligomeric and fibrillar aggregates generated by these peptides are amongst the principal components of amyloid plaques found post mortem in patients suffering from AD. Rosmarinic acid has been demonstrated to be effective in preventing the aggregation of amyloid peptides in vitro and to delay the progression of the disease in animal models. Nevertheless, no information is available about its molecular mechanism of action. Herein, we report the NMR characterization of the interaction of <jats:italic>Salvia sclareoides<\/jats:italic> extract and that of its major component, rosmarinic acid, with A\u03b21\u201342 peptide, whose oligomers have been described as the most toxic A\u03b2 species in vivo. Our data shed light on the structural determinants of rosmarinic acid\u2013A\u03b21\u201342 oligomers interaction, thus allowing the elucidation of its mechanism of action. They also provide important information for the rational design of new compounds with higher affinity for A\u03b2 peptides to generate new anti\u2010amyloidogenic molecules and\/or molecular tools for the specific targeting of amyloid aggregates in vivo. In addition, we identified methyl caffeate, another natural compound present in different plants and human diet, as a good ligand of A\u03b21\u201342 oligomers, which also shows anti\u2010amyloidogenic activity. Finally, we demonstrated the possibility to exploit STD\u2010NMR and trNOESY experiments to screen extracts from natural sources for the presence of A\u03b2 peptide ligands.<\/jats:p>","DOI":"10.1002\/asia.201201063","type":"journal-article","created":{"date-parts":[[2013,1,9]],"date-time":"2013-01-09T16:05:48Z","timestamp":1357747548000},"page":"596-602","source":"Crossref","is-referenced-by-count":82,"title":["Natural Compounds against Alzheimer\u2019s Disease: Molecular Recognition of A\u03b21\u201342 Peptide by <i>Salvia sclareoides<\/i> Extract and its Major Component, Rosmarinic Acid, as Investigated by NMR"],"prefix":"10.1002","volume":"8","author":[{"given":"Cristina","family":"Airoldi","sequence":"first","affiliation":[]},{"given":"Erika","family":"Sironi","sequence":"additional","affiliation":[]},{"given":"Catarina","family":"Dias","sequence":"additional","affiliation":[]},{"given":"Filipa","family":"Marcelo","sequence":"additional","affiliation":[]},{"given":"Alice","family":"Martins","sequence":"additional","affiliation":[]},{"given":"Am\u00e9lia Pilar","family":"Rauter","sequence":"additional","affiliation":[]},{"given":"Francesco","family":"Nicotra","sequence":"additional","affiliation":[]},{"given":"Jesus","family":"Jimenez\u2010Barbero","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2013,1,9]]},"reference":[{"key":"e_1_2_6_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1474-4422(04)00853-1"},{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(84)80190-4"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.2165\/00002512-199915050-00004"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.3233\/JAD-2009-1044"},{"key":"e_1_2_6_5_2","unstructured":"\u00a0"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.2174\/092986710791959729"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.2174\/157340711796817896"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbr.2007.03.001"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0031-9422(98)00730-4"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1124\/jpet.105.099317"},{"key":"e_1_2_6_11_2","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.1002\/(SICI)1521-3757(19990614)111:12<1902::AID-ANGE1902>3.0.CO;2-O","volume":"111","author":"Meyer M. 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