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. 2024 Sep 3;14:20508. doi: 10.1038/s41598-024-71446-8

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 1 — Workflow for assessment of TTR stability under urea conditions. TTR-containing samples were diluted tenfold with PBS containing 0–8 mol/L urea, resulting in a final concentration of 0–7.2 mol/L urea, and incubated at 25 °C for 48 h. After incubation, the samples were diluted 6180 times with PBS containing 1% BSA and applied to ELISA plate wells immediately after dilution. Tetrameric TTR levels in the samples were quantified via ELISA in duplicate. TTR stability under urea conditions was evaluated as the residual TTR tetramer percentage. ATTRwt, wild-type transthyretin amyloidosis; TTR, transthyretin; ELISA, enzyme-linked immunosorbent assay.