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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2023,5,30]]},"abstract":"<jats:p>\n                    The assembly of the \u03b2-amyloid peptide (A\u03b2) to form oligomers and fibrils is closely associated with the pathogenesis and progression of Alzheimer\u2019s disease. A\u03b2 is a shape-shifting peptide capable of adopting many conformations and folds within the multitude of oligomers and fibrils the peptide forms. These properties have precluded detailed structural elucidation and biological characterization of homogeneous, well-defined A\u03b2 oligomers. In this paper, we compare the structural, biophysical, and biological characteristics of two different covalently stabilized isomorphic trimers derived from the central and\n                    <jats:italic>C<\/jats:italic>\n                    -terminal regions A\u03b2. X-ray crystallography reveals the structures of the trimers and shows that each trimer forms a ball-shaped dodecamer. Solution-phase and cell-based studies demonstrate that the two trimers exhibit markedly different assembly and biological properties. One trimer forms small soluble oligomers that enter cells through endocytosis and activate capase-3\/7-mediated apoptosis, while the other trimer forms large insoluble aggregates that accumulate on the outer plasma membrane and elicit cellular toxicity through an apoptosis-independent mechanism. The two trimers also exhibit different effects on the aggregation, toxicity, and cellular interaction of full-length A\u03b2, with one trimer showing a greater propensity to interact with A\u03b2 than the other. The studies described in this paper indicate that the two trimers share structural, biophysical, and biological characteristics with oligomers of full-length A\u03b2. The varying structural, assembly, and biological characteristics of the two trimers provide a working model for how different A\u03b2 trimers can assemble and lead to different biological effects, which may help shed light on the differences among A\u03b2 oligomers.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2219216120","type":"journal-article","created":{"date-parts":[[2023,5,22]],"date-time":"2023-05-22T15:02:10Z","timestamp":1684767730000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":18,"title":["Probing differences among A\u03b2 oligomers with two triangular trimers derived from A\u03b2"],"prefix":"10.1073","volume":"120","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9724-6298","authenticated-orcid":false,"given":"Adam G.","family":"Kreutzer","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of California Irvine, Irvine, CA 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