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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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In the context of the P301L/S320F aggregation mutations, K321Q and K353Q acetylmimetics disrupt conformational amyloid structure as shown by reduced Thioflavin reactivity. (A) HEK293T cells were transfected to express WT, P301L/S320F, P301L/S320F/K321Q, P301L/S320F/K353Q, or P301L/S320F/K321Q/K353Q 0N4R tau. Cells were plated onto slides and labeled for fluorescence with DAPI for nuclei, 3026 antibody/Alexa 594 for total tau (red), and Thioflavin S for amyloid structure (green). (B) Graph shows the ratio of thioflavin positive to tau positive cells calculated from 10 different ×20 fields for each group. One-way ANOVA with Dunnett’s test was performed with N = 10 for WT tau and mutations. ****p < 0.0001. Scale bar = 50 µm.