{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T12:42:11Z","timestamp":1792672931904,"version":"4.5.0"},"reference-count":64,"publisher":"American Chemical Society (ACS)","issue":"42","license":[{"start":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T00:00:00Z","timestamp":1787788800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T00:00:00Z","timestamp":1787788800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T00:00:00Z","timestamp":1787788800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100006940","name":"University of Mississippi","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006940","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004312","name":"Eli Lilly and Company","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004312","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014455","name":"University of Tennessee, Knoxville","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014455","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Early tau assembly intermediates are increasingly recognized as bioactive species that govern downstream aggregation and cellular dysfunction, yet it remains unresolved whether distinct tau fragments directly interact during these early stages to redirect pathway selection. Here, we use a cofactor-free two-peptide model, TauPHF43 and jR2R3P301L, to test whether fragments that share the PHF6 amyloidogenic motif but differ in sequence context coassemble before mature fibrils emerge. Recent cryo-EM work established heparin-induced jR2R3P301L fibrils as a minimal 4R tau-prion model; our study instead probes the early cofactor-free assembly landscape of this peptide and its remodeling by TauPHF43. We find that jR2R3P301L rapidly forms heterogeneous higher-order oligomers and short, bundled fibrils that reduce the CCK-8 signal in HEK293 and HMC3 cells. Experimental data and candidate models support compact strand\u2013loop\u2013strand-like assembly states, including a putative conversion-limited hexamer. TauPHF43 is largely monomeric and nonfibrillogenic in isolation but forms jR2R3P301L-rich hetero-oligomers. A candidate [2 + 8] model qualitatively suggests that peripheral TauPHF43 association may favor an extended jR2R3P301L scaffold, consistent with the longer, thinner fibrils observed in the mixture. Coassembly also modifies CCK-8 responses in a cell-type-dependent manner. These findings support early hetero-oligomerization as one mechanism by which local sequence context and cross-fragment interactions can reshape tau assembly pathways and generate structural and biological heterogeneity.<\/jats:p>","DOI":"10.1021\/acs.jpcb.6c05345","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T18:01:17Z","timestamp":1788285677000},"page":"11166-11177","source":"Crossref","is-referenced-by-count":0,"title":["Early Hetero-Oligomerization\nof Tau Fragments Redirects\nCofactor-Free Tau Assembly and Fibril Morphology"],"prefix":"10.1021","volume":"130","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-8275-6406","authenticated-orcid":true,"given":"Happy Abena","family":"Safoah","sequence":"first","affiliation":[{"name":"University of Tennessee , , , ,","place":["Knoxville, Tennessee, United States, 37996"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah S.","family":"Hirschbeck","sequence":"additional","affiliation":[{"name":"University of Tennessee , , , ,","place":["Knoxville, Tennessee, United States, 37996"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jie","family":"Chen","sequence":"additional","affiliation":[{"name":"University of Mississippi , , , ,","place":["University, Mississippi, United States, 38677"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neus","family":"Domingo","sequence":"additional","affiliation":[{"name":"Oak Ridge National Laboratory , , , ,","place":["Oak Ridge, Tennessee, United States, 37831"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilana","family":"Sogolovsky-Bard","sequence":"additional","affiliation":[{"name":"Tel Aviv University , , ,","place":["Tel Aviv, Israel, 6997801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ava","family":"Sams","sequence":"additional","affiliation":[{"name":"University of Tennessee , , , ,","place":["Knoxville, Tennessee, United States, 37996"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adit","family":"Harish","sequence":"additional","affiliation":[{"name":"University of Tennessee , , , ,","place":["Knoxville, Tennessee, United States, 37996"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miriam J.","family":"Melkonian","sequence":"additional","affiliation":[{"name":"Westmont College , , , ,","place":["Santa Barbara, California, United States, 93108"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristi","family":"Lazar Cantrell","sequence":"additional","affiliation":[{"name":"Westmont College , , , ,","place":["Santa Barbara, California, United States, 93108"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dana","family":"Laor Bar-Yosef","sequence":"additional","affiliation":[{"name":"Tel Aviv University , , ,","place":["Tel Aviv, Israel, 6997801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5764-1720","authenticated-orcid":true,"given":"Ehud","family":"Gazit","sequence":"additional","affiliation":[{"name":"Tel Aviv University , , ,","place":["Tel Aviv, Israel, 6997801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5064-761X","authenticated-orcid":true,"given":"Jinchao","family":"Lou","sequence":"additional","affiliation":[{"name":"University of Mississippi , , , ,","place":["University, Mississippi, United States, 38677"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1978-4365","authenticated-orcid":true,"given":"Thanh D.","family":"Do","sequence":"additional","affiliation":[{"name":"University of Tennessee , , , ,","place":["Knoxville, Tennessee, United States, 37996"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,27]]},"reference":[{"issue":"12","key":"2026102207413883600_cit1","doi-asserted-by":"publisher","DOI":"10.1172\/jci168553","article-title":"Tau pathology in\nneurodegenerative disease: disease mechanisms and therapeutic avenues","volume":"133","author":"Samudra","year":"2023","journal-title":"J. Clin. Invest."},{"issue":"23","key":"2026102207413883600_cit2","doi-asserted-by":"publisher","first-page":"2316","DOI":"10.1001\/jama.2019.7437","article-title":"Associations of Amyloid, Tau, and Neurodegeneration\nBiomarker Profiles With Rates of Memory Decline Among Individuals\nWithout Dementia","volume":"321","author":"Jack","year":"2019","journal-title":"JAMA"},{"key":"2026102207413883600_cit3","doi-asserted-by":"publisher","first-page":"25","DOI":"10.3389\/fnins.2018.00025","article-title":"Reconsideration of Amyloid Hypothesis\nand Tau Hypothesis\nin Alzheimer\u2019s Disease","volume":"12","author":"Kametani","year":"2018","journal-title":"Front. Neurosci."},{"issue":"4","key":"2026102207413883600_cit4","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1001\/jamaneurol.2013.5847","article-title":"Amyloid-beta\nand tau: the trigger and bullet in Alzheimer disease pathogenesis","volume":"71","author":"Bloom","year":"2014","journal-title":"JAMA Neurol"},{"issue":"1","key":"2026102207413883600_cit5","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1038\/s41583-019-0240-3","article-title":"Amyloid-beta-independent\nregulators of tau pathology in Alzheimer disease","volume":"21","author":"van der Kant","year":"2020","journal-title":"Nat. Rev. Neurosci."},{"issue":"12","key":"2026102207413883600_cit6","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1038\/s41582-023-00883-2","article-title":"Tau-targeting\ntherapies for Alzheimer disease: current status and future directions","volume":"19","author":"Congdon","year":"2023","journal-title":"Nat. Rev. Neurol."},{"key":"2026102207413883600_cit7","doi-asserted-by":"publisher","first-page":"595532","DOI":"10.3389\/fneur.2020.595532","article-title":"Tau Post-translational\nModifications:\nDynamic Transformers of Tau Function, Degradation, and Aggregation","volume":"11","author":"Alquezar","year":"2021","journal-title":"Front. Neurol."},{"issue":"1","key":"2026102207413883600_cit8","doi-asserted-by":"publisher","first-page":"3706","DOI":"10.1038\/s41467-023-39328-1","article-title":"Specific post-translational modifications of soluble\ntau protein distinguishes Alzheimer\u2019s disease and primary tauopathies","volume":"14","author":"Kyalu Ngoie Zola","year":"2023","journal-title":"Nat. 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Int."},{"issue":"25","key":"2026102207413883600_cit10","doi-asserted-by":"publisher","first-page":"6207","DOI":"10.1016\/j.cell.2021.11.029","article-title":"Posttranslational\nModifications Mediate the Structural Diversity of Tauopathy Strains","volume":"184","author":"Arakhamia","year":"2021","journal-title":"Cell"},{"key":"2026102207413883600_cit11","doi-asserted-by":"publisher","DOI":"10.7554\/elife.43584","article-title":"Heparin-induced tau filaments are\npolymorphic and differ from those in Alzheimer\u2019s and Pick\u2019s\ndiseases","volume":"8","author":"Zhang","year":"2019","journal-title":"eLife"},{"issue":"4","key":"2026102207413883600_cit12","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1021\/acssensors.0c00193","article-title":"Mechanisms of Heparin-Induced Tau Aggregation Revealed by a Single\nNanopore","volume":"5","author":"Giamblanco","year":"2020","journal-title":"ACS Sens."},{"issue":"6","key":"2026102207413883600_cit13","doi-asserted-by":"publisher","first-page":"3592","DOI":"10.1074\/jbc.M109.035691","article-title":"Quantitative characterization\nof heparin binding to Tau protein: implication for inducer-mediated\nTau filament formation","volume":"285","author":"Zhu","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"4","key":"2026102207413883600_cit14","doi-asserted-by":"publisher","first-page":"4729","DOI":"10.1021\/jacs.5c22156","article-title":"Dopamine-Induced Tau\nModification Prevents Pathological Phosphorylation and Generates a\nDistinct Fibril Polymorph","volume":"148","author":"Liu","year":"2026","journal-title":"J. Am. Chem. Soc."},{"key":"2026102207413883600_cit15","doi-asserted-by":"publisher","first-page":"1181804","DOI":"10.3389\/fnins.2023.1181804","article-title":"Tau mutation S356T\nin the three repeat isoform leads to microtubule dysfunction and promotes\nprion-like seeded aggregation","volume":"17","author":"Xia","year":"2023","journal-title":"Front. Neurosci."},{"issue":"8","key":"2026102207413883600_cit16","doi-asserted-by":"publisher","first-page":"1470","DOI":"10.1038\/s41594-025-01575-9","article-title":"Distinct tau filament\nfolds in human MAPT mutants P301L and P301T","volume":"32","author":"Schweighauser","year":"2025","journal-title":"Nat. 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Chem."},{"issue":"7","key":"2026102207413883600_cit23","doi-asserted-by":"publisher","first-page":"112725","DOI":"10.1016\/j.celrep.2023.112725","article-title":"Super-resolution\nimaging unveils the self-replication of tau aggregates upon seeding","volume":"42","author":"Dimou","year":"2023","journal-title":"Cell Rep."},{"issue":"41","key":"2026102207413883600_cit24","doi-asserted-by":"publisher","first-page":"E4376","DOI":"10.1073\/pnas.1411649111","article-title":"Proteopathic tau\nseeding predicts tauopathy in vivo","volume":"111","author":"Holmes","year":"2014","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"issue":"15","key":"2026102207413883600_cit25","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2320456121","article-title":"Precision proteoform\ndesign for 4R tau isoform selective templated aggregation","volume":"121","author":"Longhini","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. 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Struct. Biol."},{"issue":"22","key":"2026102207413883600_cit31","doi-asserted-by":"publisher","first-page":"169008","DOI":"10.1016\/j.jmb.2025.169008","article-title":"How is the Amyloid\nFold Built? Polymorphism and the\nMicroscopic Mechanisms of Fibril Assembly","volume":"437","author":"Aubrey","year":"2025","journal-title":"J.\nMol. Biol."},{"issue":"18","key":"2026102207413883600_cit32","doi-asserted-by":"publisher","first-page":"5922","DOI":"10.1021\/ja7100517","article-title":"Characterization of Alzheimer\u2019s-like\npaired helical filaments from the core domain of tau protein using\nsolid-state NMR spectroscopy","volume":"130","author":"Andronesi","year":"2008","journal-title":"J. Am. Chem. Soc."},{"issue":"40","key":"2026102207413883600_cit33","doi-asserted-by":"publisher","first-page":"10526","DOI":"10.1021\/bi800783d","article-title":"The natively\nunfolded character of tau and its aggregation to Alzheimer-like paired\nhelical filaments","volume":"47","author":"Jeganathan","year":"2008","journal-title":"Biochemistry"},{"issue":"13","key":"2026102207413883600_cit34","doi-asserted-by":"publisher","first-page":"4582","DOI":"10.1021\/acs.jpcb.5b00175","article-title":"Tau assembly:\nthe dominant role of PHF6 (VQIVYK) in microtubule binding region repeat\nR3","volume":"119","author":"Ganguly","year":"2015","journal-title":"J. Phys. Chem. 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Neurosci."},{"issue":"13","key":"2026102207413883600_cit37","doi-asserted-by":"publisher","first-page":"5115","DOI":"10.1021\/acs.analchem.3c04974","article-title":"Exploring the Aggregation Propensity\nof PHF6 Peptide Segments of the Tau Protein Using Ion Mobility Mass\nSpectrometry Techniques","volume":"96","author":"Stroganova","year":"2024","journal-title":"Anal. Chem."},{"issue":"14","key":"2026102207413883600_cit38","doi-asserted-by":"publisher","first-page":"2339","DOI":"10.1016\/j.bpj.2025.06.009","article-title":"Intrinsic\naggregation and propagation of unmodified tau peptides: R2R3 as a\nminimal model system","volume":"124","author":"Das","year":"2025","journal-title":"Biophys. J."},{"issue":"18","key":"2026102207413883600_cit39","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2421391122","article-title":"Water-directed\npinning is key to tau prion formation","volume":"122","author":"Vigers","year":"2025","journal-title":"Proc.\nNatl. Acad. Sci. U. S. 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