Nε-(carboxymethyl)lysine promotes lipid uptake of macrophage via cluster of differentiation 36 and receptor for advanced glycation end products

Figure 2 N^ε-(carboxymethyl)lysine has a higher binding affinity to cluster of differentiation 36 than to receptor for advanced glycation end products. A and B: Detection of N^ε-(carboxymethyl)lysine (CML) binding to cluster of differentiation 36 (CD36) (A) and to receptor for advanced glycation end products (RAGE) (B) by immunoprecipitation; C: Synthesis of N-succinimidyl-4-¹⁸F-fluorobenzoate-CML; D and E: Detection of the specific binding between CML and CD36 (D) and between CML and RAGE (E) with radioreceptor ligand binding assays; F: Molecular docking model of CML-CD36 binding; G: Detail of the binding site of CML to CD36; H: Amino acids for the binding interaction between CML and CD36. SB: Specific binding; NB: Non-specific binding; TB: Total binding. CPM: Counts/minute.