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This knowledge has prompted us to design and optimize a rapid and simple high\u2010throughput assay that relies on the ability of test compounds to form ternary soluble complexes TTR\/A\u03b2\/SMC that prevent A\u03b2 aggregation. The method uses the shorter A\u03b2(12\u201328) sequence which is cheaper and simpler to use while retaining the aggregation properties of their parents A\u03b2(1\u201340) and A\u03b2(1\u201342). The test is carried out in 96\u2010plate wells that are UV monitored for turbidity during 6\u2005h. Given its reproducibility, we propose that this test can be a powerful tool for efficient screening of SMCs that act as chaperones of the TTR\/A\u03b2 interaction that may led to potential AD therapies.<\/jats:p>","DOI":"10.1002\/chem.202002933","type":"journal-article","created":{"date-parts":[[2020,8,6]],"date-time":"2020-08-06T15:35:49Z","timestamp":1596728149000},"page":"17462-17469","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["An Assay for Screening Potential Drug Candidates for Alzheimer's Disease That Act as Chaperones of the Transthyretin and Amyloid\u2010\u03b2 Peptides Interaction"],"prefix":"10.1002","volume":"26","author":[{"given":"Ellen Y.","family":"Cotrina","sequence":"first","affiliation":[{"name":"Institut de Qu\u00edmica Avan\u00e7ada de Catalunya (I.Q.A.C.-C.S.I.C.)  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