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. 2019 Nov 20;9:17123. doi: 10.1038/s41598-019-53388-8

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Ability of CD36 variants to bind ligand. Cells were transfected with constructs coding for CD36-wild type (A), CD36-p.Pro191Leu (B) and CD36-p.Aal252Val (C). Bound acLDL was measured by fluorescent-detection of the BODIPY fluorophore. Data points for each acLDL concentration were normalized internally for each transfection against 0μgml⁻¹ acLDL, plotted alongside the corresponding values for an unstransfected (UT) control and best-fitted using a Langmuir adsorption isotherm equation for one-site binding. Each dataset represents the mean of three biological replicates and error bars describe standard error of the mean. Mean Kd values show no statistical difference in equilibrium binding of acLDL (D).