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. 2024 Dec 3;14:30050. doi: 10.1038/s41598-024-80897-y

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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. 6 — Congo Red (CR) binding was performed to detect the amyloid fibrils in solution. The absorbance spectra of α-LA (0.2 mg mL⁻¹) were obtained under different conditions, such as CR binding at pH 7.0 () and pH 2.0 () in the presence of 0.2 (), 0.3 (), and 0.5 () mM SHMP at pH 2.0. A fixed amount of CR (10 µM) was added to both the aggregated and nonaggregated samples and incubated for 30 min in the dark prior to the measurements.

Inline graphic — Congo Red (CR) binding was performed to detect the amyloid fibrils in solution. The absorbance spectra of α-LA (0.2 mg mL⁻¹) were obtained under different conditions, such as CR binding at pH 7.0 () and pH 2.0 () in the presence of 0.2 (), 0.3 (), and 0.5 () mM SHMP at pH 2.0. A fixed amount of CR (10 µM) was added to both the aggregated and nonaggregated samples and incubated for 30 min in the dark prior to the measurements.