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Its biological relevance is highlighted by its co\u2010localization with amyloid\u2010\u03b2 (A\u03b2) deposits in both Alzheimer's disease patients and transgenic mice models. Notably, Medin promotes amyloid\u2010\u03b2 aggregation, forming mixed fibrils with A\u03b2 and enhancing its deposition in blood vessels. Here we report a new and efficient strategy to chemically access this compound. Our approach employs a solubilizing linker that not only ensures high solubility but also suppresses aggregation, allowing efficient purification of the product. The linker can be removed without a trace, after which the product behaves identically to wild\u2010type Medin and forms amyloid fibrils. The synthesis route allows opening up a new chemical space, including nonnatural modifications like biotinylation. Together with the control over the aggregation properties, this is a powerful tool for amyloid protein studies.<\/jats:p>","DOI":"10.1002\/psc.70041","type":"journal-article","created":{"date-parts":[[2025,7,14]],"date-time":"2025-07-14T00:01:01Z","timestamp":1752451261000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Chemical Synthesis of Medin via a Removable Aggregation\u2010Suppressing Linker"],"prefix":"10.1002","volume":"31","author":[{"given":"Matthias","family":"De\u00a0Vleeschouwer","sequence":"first","affiliation":[{"name":"Switch Laboratory VIB Center for Brain and Disease Research  Leuven Belgium"},{"name":"Department for Cellular and Molecular Medicine KU Leuven  Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brajabandhu","family":"Pradhan","sequence":"additional","affiliation":[{"name":"Switch Laboratory VIB Center for Brain and Disease Research  Leuven Belgium"},{"name":"Department for Cellular and Molecular Medicine KU Leuven  Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9189-7399","authenticated-orcid":false,"given":"Frederic","family":"Rousseau","sequence":"additional","affiliation":[{"name":"Switch Laboratory VIB Center for Brain and Disease Research  Leuven Belgium"},{"name":"Department for Cellular and Molecular Medicine KU Leuven  Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2020-0168","authenticated-orcid":false,"given":"Joost","family":"Schymkowitz","sequence":"additional","affiliation":[{"name":"Department for Cellular and Molecular Medicine KU Leuven  Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,7,13]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2012.02.022"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41580-018-0060-8"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1080\/13506129.2020.1835263"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.15.8669"},{"key":"e_1_2_5_6_1","first-page":"871","article-title":"Senile Aortic Amyloid. 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