CD36 Inhibitors

CD36, also known as platelet glycoprotein IV, is a multifunctional transmembrane protein found on the surface of various cell types, including platelets, monocytes, adipocytes, and endothelial cells. It belongs to the class B scavenger receptor family and is implicated in a variety of biological processes such as lipid uptake, angiogenesis, inflammation, and cell adhesion. Structurally, CD36 is characterized by its two transmembrane domains, with both the N-terminal and C-terminal ends located intracellularly. The large extracellular loop contains ligand-binding sites that allow CD36 to interact with a diverse range of molecules, including long-chain fatty acids, oxidized low-density lipoproteins (oxLDL), and thrombospondin-1. CD36 inhibitors are chemical entities that specifically block or modulate the function of the CD36 receptor. Given the receptor's diverse ligand-binding capabilities, the inhibition of CD36 can have varied effects depending on the context. For instance, by blocking the binding of oxLDL to CD36, these inhibitors reduce lipid uptake and foam cell formation, which are critical steps in the development of atherosclerosis. Similarly, inhibiting CD36-mediated fatty acid uptake can impact lipid metabolism and energy homeostasis in cells. The design and synthesis of CD36 inhibitors often hinge on understanding the molecular interactions between CD36 and its ligands, allowing for the creation of molecules that can effectively compete with natural ligands for binding. Various compounds, ranging from small molecules to peptides, have been explored for their ability to inhibit CD36 function. These inhibitors not only advance our understanding of CD36's role in physiological and pathophysiological processes but also provide a platform for further explorations into the myriad cellular pathways influenced by this versatile receptor.