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. 2021 Aug 23;11:17069. doi: 10.1038/s41598-021-96627-7

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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K321Q and K353Q tau acetylmimetics inhibit prion-like seeded aggregation in the context of P301L mutation. Cell-based tau inclusion assays were used to determine aggregation and prion-like seeding of (A) 0N4R WT tau, and (B) P301L, (C) K259Q/P301L, (D) K290Q/P301L, (E) K321Q/P301L/, and (F) K353Q/ P301L 0N4R tau. Immunoblots were probed with tau antibody 3026. The relative molecular weight markers are shown on the left. (G) One-way ANOVA with Dunnett’s test was performed with N = 3 for WT tau and all mutations. ****p < 0.0001 and ns not statistically significant.