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Anti-A\u03b2 antibodies (A\u03b2-Abs) targeting specific A\u03b2 variants are essential tools for AD research, diagnostics, and therapy. The monoclonal antibodies Aducanumab, Lecanemab, and Donanemab have recently been approved as the first disease-modifying treatments for early AD, highlighting the clinical importance of their exact binding profiles. In this study, we systematically characterized the binding and modification requirements of 20 A\u03b2-Abs, including biosimilars of Aducanumab, Lecanemab, and Donanemab, across monomeric, oligomeric, and aggregated A\u03b2 forms. Array-based analysis of 20,000 modified A\u03b2 peptides defined binding epitopes at single-residue resolution and revealed the impact of sequence variation, including familial AD mutations, as well as diverse post-translational modifications (PTMs). Notably, genetic variants, such as H6R, impaired binding of therapeutic A\u03b2-Abs like Aducanumab. Donanemab showed strong preference for pyroglutamate-modified A\u03b2pE3\u201317, while Lecanemab and Aducanumab exhibited aggregation- and sequence-context-dependent binding requirements. Comparison of peptide binding profiles with binding of full-length and aggregated A\u03b2 via immunoprecipitation-mass spectrometry, capillary immunoassays, Western blotting, and immunohistochemistry on AD brain tissue revealed distinct aggregation-dependent binding behaviours. The valency- and context-dependence of Aducanumab binding, together with its preference for Ser8-phosphorylated A\u03b2, supports a dimerization-mediated binding mechanism. For Lecanemab, our data suggest that additional structural contributions beyond the minimal N-terminal epitope are required for binding to aggregated A\u03b2, which remain to be fully resolved. Together, this work provides the most comprehensive dataset to date on aggregation-dependent sequence and modification selectivity of A\u03b2-Abs. By integrating mutational, PTM, and aggregation contexts in a unified experimental framework, we establish a resource that enables rational selection of antibodies for research and diagnostic applications and offers mechanistic insights that may inform the design and optimization of future therapeutic antibodies in AD.<\/jats:p>","DOI":"10.7554\/elife.106156","type":"journal-article","created":{"date-parts":[[2025,5,9]],"date-time":"2025-05-09T10:30:38Z","timestamp":1746786638000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.106156","source":"Crossref","is-referenced-by-count":5,"title":["Aggregation-dependent epitope sequence and modification fingerprints of anti-A\u03b2 antibodies"],"prefix":"10.7554","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5617-8869","authenticated-orcid":true,"given":"Ivan","family":"Talucci","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00fbnyb24","id-type":"ROR","asserted-by":"publisher"}],"name":"Rudolf Virchow 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