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. 2021 Sep 27;11:19125. doi: 10.1038/s41598-021-98243-x

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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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Isothermal titration calorimetric (ITC) profile of the binding between CCM and NTCP. The titration of raw data between differential power (DP, µcal/s) and time (min) after sequential injection of ligand (150 μM CCM) into the protein solution (15 μM of NTCP, pH 7.0, 25 °C) was plotted (A). The integrated heat after the correlation between enthalpy changes versus the molar ratios of CCM (injection) to protein (NTCP) was plotted (B). Data were fitted using a one-site binding model where the solid lines represented the best-fit results.