{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:21:41Z","timestamp":1790623301524,"version":"4.1.0"},"reference-count":249,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2020,5,23]],"date-time":"2020-05-23T00:00:00Z","timestamp":1590192000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010661","name":"Horizon 2020","doi-asserted-by":"publisher","award":["860070"],"award-info":[{"award-number":["860070"]}],"id":[{"id":"10.13039\/100010661","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Alzheimer\u2019s disease (AD) represents a progressive amyloidogenic disorder whose advancement is widely recognized to be connected to amyloid-\u03b2 peptides and Tau aggregation. However, several other processes likely contribute to the development of AD and some of them might be related to protein-protein interactions. Amyloid aggregates usually contain not only single type of amyloid protein, but also other type of proteins and this phenomenon can be rationally explained by the process of protein cross-seeding and co-assembly. Amyloid cross-interaction is ubiquitous in amyloid fibril formation and so a better knowledge of the amyloid interactome could help to further understand the mechanisms of amyloid related diseases. In this review, we discuss about the cross-interactions of amyloid-\u03b2 peptides, and in particular A\u03b21-42, with other amyloids, which have been presented either as integrated part of A\u03b2 neurotoxicity process (such as Tau) or conversely with a preventive role in AD pathogenesis by directly binding to A\u03b2 (such as transthyretin, cystatin C and apolipoprotein A1). Particularly, we will focus on all the possible therapeutic strategies aiming to rescue the A\u03b2 toxicity by taking inspiration from these protein-protein interactions.<\/jats:p>","DOI":"10.3390\/molecules25102439","type":"journal-article","created":{"date-parts":[[2020,5,25]],"date-time":"2020-05-25T11:42:02Z","timestamp":1590406922000},"page":"2439","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":66,"title":["The Positive Side of the Alzheimer\u2019s Disease Amyloid Cross-Interactions: The Case of the A\u03b2 1-42 Peptide with Tau, TTR, CysC, and ApoA1"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2762-1929","authenticated-orcid":false,"given":"Lidia","family":"Ciccone","sequence":"first","affiliation":[{"name":"Department of Pharmacy, University of Pisa, via Bonanno 6, 56126 Pisa, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chenghui","family":"Shi","sequence":"additional","affiliation":[{"name":"CNRS, BioCIS, Universit\u00e9 Paris-Saclay, rue Jean-Baptiste Cl\u00e9ment 5, 92290 Ch\u00e2tenay-Malabry, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Davide","family":"di Lorenzo","sequence":"additional","affiliation":[{"name":"CNRS, BioCIS, Universit\u00e9 Paris-Saclay, rue Jean-Baptiste Cl\u00e9ment 5, 92290 Ch\u00e2tenay-Malabry, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne-C\u00e9cile","family":"Van Baelen","sequence":"additional","affiliation":[{"name":"D\u00e9partement M\u00e9dicaments et Technologies pour la Sant\u00e9 (DMTS), CEA, INRAE, Universit\u00e9 Paris Saclay, SIMoS, 91191 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1435-5676","authenticated-orcid":false,"given":"Nicolo","family":"Tonali","sequence":"additional","affiliation":[{"name":"CNRS, BioCIS, Universit\u00e9 Paris-Saclay, rue Jean-Baptiste Cl\u00e9ment 5, 92290 Ch\u00e2tenay-Malabry, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,5,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/joim.12506","article-title":"Current and future treatment of amyloid diseases","volume":"280","author":"Ankarcrona","year":"2016","journal-title":"J. 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